Recombinant Human CD9 Protein (C-6His)

Name: Recombinant Human CD9 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-2585NP
Availability: InStock

BL-2585NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Cluster of differentiation (cd) proteins, Featured cd protein molecules, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human CD9 Antigen is produced by our Mammalian expression system and the target gene encoding Ser112-Ile195 is expressed with a 6His tag at the C-terminus.
Accession	P21926
Synonym	CD9 antigen; CD9 molecule; CD9; Cell growth-inhibiting gene 2 protein; MIC3; TSPAN29; DRAP-27; MRP1; BTCC1
Gene Background	CD9, also known as Tspan29, 5H9 antigen, Leukocyte antigen MIC3 (MIC3), Motility-related protein, is a multi-pass membrane protein which belongs to the tetraspanin (TM4SF) family or the transmembrane 4 superfamily. CD9 is a cell surface glycoprotein with 4 hydrophobic domains that is described to complex with integrins and other transmembrane 4 superfamily members. The protein takes part in cellular signal transduction events and thus play a role in the regulation of cell development and activation, growth and motility. Besides, CD9 seems to be a key role in the egg-sperm fusion during the mammalian fertilization processes. CD9 also seems to be a key part in the egg-sperm fusion during mammalian fertilization.
Molecular Mass	10.5 KDa
Apmol Mass	11 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion. Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion. In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration. In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption. Acts as a receptor for PSG17. Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis.
Subcellular Location	Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein. Secreted, extracellular exosome.
Protein Families	Tetraspanin (TM4SF) family
Database References	HGNC: 1709 OMIM: 143030 KEGG: hsa:928 STRING: 9606.ENSP00000009180 UniGene: Hs.114286
Tissue Specificity	Detected in platelets (at protein level). Expressed by a variety of hematopoietic and epithelial cells.

Gene Functions References

assays. Results from the present study demonstrated that CD9 was highly expressed in the highly metastatic Hepatocellular carcinoma (HCC)cells and promoted HCC cell migration. This protein may be a novel target for regulating the invasive phenotype in HCC. PMID: 29749468
The species-specific traits in CD9 and CD81 distribution during sperm maturation were compared between mice and humans. A mutual position of CD9/CD81 is shown in human spermatozoa in the acrosomal cap, however in mice, CD9 and CD81 occupy a distinct area. PMID: 29671763
CD9 expression predicts some clinical characteristics and indicates an unfavorable prognosis in acute lymphoblastic leukemia patients. PMID: 29286918
CD9-CD81 blockage reduces exosome-mediated HIV-1 entry. PMID: 29429034
Exosomal markers CD63 and CD9 are elevated in pancreatic tumor tissues. PMID: 28609367
CD9 expression could be a biomarker for poor prognosis in invasive breast carcinoma PMID: 28178752
CD9 stabilizes gp130 by blocking its ubiquitin-dependent lysosomal degradation to promote the IL6-gp130-bone marrow X-linked non-receptor tyrosine kinase-STAT3 signaling for maintaining GSC selfrenewal and tumorigenic capacity. PMID: 27740621
CD9 was highly expressed on extravillous trophoblast (EVT) at the boundary region of EVT invasion and intravascular EVT. CD9 expression on Swan71 cells was reduced under hypoxic conditions, while its expression was increased by co-culture with HUVEC. CD9 could attenuate EVT invasion under the influence of an oxygen environment and maternal endothelial cells, proposing CD9 as a potential regulator of human placentation. PMID: 27780531
As for 18Lin(-), CD34(-) HSCs are characterized by low expression of the tetraspanin CD9, which promotes homing, and high expression of the peptidase CD26, which inhibits homing. PMID: 28687990
The findings suggest that, in contrast with previous models, the ligand-binding site of integrin alphaVbeta3, binds to the constant region (helices A and B) of the EC2 domain of CD9, CD81, and CD151 antigens. PMID: 27993971
Data suggest that CD9 should be further evaluated as a target for glioblastoma treatment. PMID: 26573230
Collectively, using tetraspanin CD9 in tandem with E-cadherin as a biomarker in renal cell carcinoma will help to not only distinguish between types, but also predict the metastatic potential of RCC. PMID: 26855131
Data indicate that CD9 is implicated in BCC invasiveness and metastases by cellular mechanisms that involve specific CD9+ plasma membrane protrusions of BCCs. PMID: 25762645
CD9-enriched microdomains negatively regulate LPS-induced receptor formation by preventing CD14 from accumulating into lipid rafts. [Review] PMID: 26378766
Results indicate that CD9 downregulation promoted pancreatic cancer cell proliferation and migration through at least in part, enhancing the cell surface expression of EGFR. PMID: 25955689
CD9 expression is upregulated and its expression is correlated with tumor stage and lymph node metastasis in esophageal squamous cell carcinoma patients PMID: 26045817
Although the current findings did not prove any hypothesis, the indispensable role of CD9 in fertilization process was not excluded and the precise role of CD9 remains unexplained. [review] PMID: 25536312
CD9 plays a role in the dysmegakaryopoiesis that occurs in primary myelofibrosis. PMID: 25840601
High CD9 is associated with B acute lymphoblastic leukemia. PMID: 26320102
These results suggested that the mechanism underlying CD9-induced suppression of cell proliferation may involve the inhibition of phosphorylation of EGFR and the activity of PI3K/Akt and MAPK/Erk signaling pathways PMID: 25760022
OY-TES-1 downregulation in liver cancer cells inhibits cell proliferation by upregulating CD and downregulating NANOG. PMID: 25673160
Low levels of CD9 coincidental with a novel nonsense mutation in glycoprotein Ibbeta in a patient with Bernard-Soulier syndrome. PMID: 26275786
The cysteine residues involved in the formation of the disulfide bridges in CD9 EC2 were all essential for inhibiting multinucleated giant cell formation but a conserved glycine residue in the tetraspanin-defining 'CCG' motif was not. PMID: 25551757
alteration in CD9 expression was sufficient to profoundly disrupt cellular actin arrangement and endogenous cell contraction by interfering with RhoA signaling. PMID: 25184334
The mechanism responsible for this negative regulation exerted by CD9 on LFA-1 adhesion does not involve changes in the affinity state of this integrin but seems to be related to alterations in its state of aggregation. PMID: 26003300
The results demonstrate that hypoxia regulates CD9 expression and CD9-mediated keratinocyte migration via the p38/MAPK pathway. PMID: 25200404
Report shows that breast cancer cells contain a nuclear CD9 pool and that the abrogation of CD9 expression results in multipolar mitoses and polynucleation. PMID: 25103498
this study indicated that sialylation involved in the development of MDR of AML cells probably through ST3GAL5 or ST8SIA4 regulating the activity of PI3K/Akt signaling and the expression of P-gp and MRP1. PMID: 24531716
switch from alphavbeta5 to alphavbeta6 integrin plays a key role in CD9-regulated cell migration and MMP-9 activation in keratinocytes PMID: 25265322
High expression of CD9 was statistically associated with older patients PMID: 24553302
CD9 and CD63 tetraspanins block HIV-1-induced cell-cell fusion at the transition from hemifusion to pore opening. PMID: 24608085
Loss of CD9 expression is associated with enhancement of invasive potential of malignant mesothelioma. PMID: 24466195
CD9 and CD151 support integrin-mediated signaling at the immunological synapse. PMID: 24723389
Introduction of CD9 expression in Raji cells resulted in significantly increased cell proliferation and HDAC activity compared to mock transfected Raji cells. PMID: 24747564
Heparin-binding epidermal growth factor and CD9 are likely implicated in processes that are highly relevant for MS lesion formation PMID: 24038577
this study points to EGFR as a key mediator between CD9-mediated pro-MMP-9 release and cellular invasion of HT1080 cells. PMID: 24246676
The second extracellular loop of CD9 was responsible for the upregulation of MMP-9 production. PMID: 23840773
This is the first study of the expression and prognostic potential of the tetraspanins in oral dysplasia. PMID: 24201754
Low CD9 expression is associated with malignant mesothelioma. PMID: 23128478
Both CD9/CD81-silenced cells and CD151-silenced cells showed delayed alpha3beta1-dependent cell spreading on laminin-332. PMID: 23613949
Data indicate that CD9 acts as scaffold and assembles a ternary JAM-A-CD9-alphavbeta3 integrin complex from which JAM-A is released upon bFGF stimulation. PMID: 23389628
these data suggest that CD9 is a novel marker for a human germinal center-B cell subset that is committed to plasma cell lineage. PMID: 23291167
CD9 overexpression was confirmed in osteotropic cells. CD9 was significantly overexpressed in bone metastases versus primary tumors and visceral metastatic lesions. PMID: 23225418
tetraspanin CD9 modulates molecular organization of integrins in lymphatic endothelial cells, thereby supporting several functions required for lymphangiogenesis PMID: 23223239
Low CD9 expression is associated with gallbladder neoplasms PMID: 22613496
identifies human male germ cells with capability of long-term survival and cell turnover in the xenogeneic testis environment PMID: 22592495
Knockdown of CD9 by siRNA and blockage of CD9 activity by ALB6 in ovarian cancer cells demonstrated that constitutive activation of NF-kappaB is CD9 dependent and that CD9 is involved in anti-apoptosis PMID: 22095071
CD9 increases GCM1 expression via the cAMP/PKA signaling pathway, resulting in the increase in ERVWE1 expression. PMID: 19692500
The absence or down-regulation of CD9 expression and point mutation may play a considerable role in the pathway of the malignant transformation in the BEAS-2B cells induced by mineral powder. PMID: 17997888
CD9 associates with ADAM17 and, through this interaction, negatively regulates the sheddase activity of ADAM17. PMID: 21365281

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.