Recombinant Mouse Cd9 Antigen (CD9) Protein (His&Myc)

Name: Recombinant Mouse Cd9 Antigen (CD9) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06592P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Cluster of differentiation (cd) proteins, Featured cd protein molecules, Recombinant proteins, Recombinant proteins fall special offers - transmembrane proteins

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Product Overview

Description	Recombinant Mouse Cd9 Antigen (CD9) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P40240
Target Symbol	CD9
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	THKDEVIKELQEFYKDTYQKLRSKDEPQRETLKAIHMALDCCGIAGPLEQFISDTCPKKQLLESFQVKPCPEAISEVFNNKFHI
Expression Range	110-193aa
Protein Length	Partial
Mol. Weight	17.2 kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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 CD9 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. Also regulates integrin-dependent migration of macrophages, particularly relevant for inflammatory response in the lung.
Subcellular Location	Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein. Secreted, extracellular exosome.
Protein Families	Tetraspanin (TM4SF) family
Database References	KEGG: mmu:12527 STRING: 10090.ENSMUSP00000032492 UniGene: Mm.210676
Tissue Specificity	Expressed predominantly in the peripheral nervous system. Highly expressed in oocytes and blastocysts (at protein level). Expression is also observed on follicular oocytes in the ovary, whereas no expression is found on follicular cells (at protein level)

Gene Functions References

The Cd9(-/-) and Cd9(-/-) Cd81(-/-) deletions are associated with a decreased microvilli density on the MII oocyte surface. Microvilli thickness is significantly increased whatever the deleted tetraspanin gene be. Only Cd9 deletion clearly disturbs the vesicular traffic, increasing the number of clathrin and exosome vesicles. PMID: 27879451
CD9 regulates the T cell-stimulatory capacity of granulocyte-macrophage colony-stimulating factor (GM-CSF)-dependent bone marrow-derived Dendritic Cells (BMDCs), without affecting antigen presentation by fms-like tyrosine kinase 3 ligand (Flt3L)-dependent BMDCs. PMID: 28533221
DPP4:CD9:TTSP as the protein complexes are necessary for early efficient MERS-coronavirus entry. PMID: 28759649
Our results indicate that the suppression of cartilage degradation in CD9(-/-) could be in part related to an increase in the expression of the two main cartilage extracellular matrix proteins aggrecan and type II collagen. PMID: 27784871
upregulation may play an important role in podocyte morphology, adhesion, and migration PMID: 25503725
Tetraspanin CD9 and ectonucleotidase CD73 identify an osteochondroprogenitor population with elevated osteogenic properties. PMID: 25564652
Data indicate that anti-inflammatory effects of statins are CD9-dependent. PMID: 24040034
study demonstrates ablation of Cd9 had no detectable effect on de novo primary proatate tumour onset, but did significantly increase metastasis to the liver but not the lungs PMID: 23575960
chemotaxis toward antigen is controlled in mast cells by a cross-talk among FcepsilonRI, tetraspanin CD9, transmembrane adaptor proteins NTAL and LAT, and cytoskeleton-regulatory proteins of the ERM family PMID: 23443658
tetraspanin CD9 modulates molecular organization of integrins in lymphatic endothelial cells, thereby supporting several functions required for lymphangiogenesis PMID: 23223239
Tetraspanin family member CD9 plays an important role in sperm-egg fusion. PMID: 22609062
Results show that SSCs are the most concentrated in CD9(+)EPCAM(low/-) population and also suggest that EPCAM plays an important role in progenitor cell amplification in the mouse spermatogenic system. PMID: 21858196
Our study demonstrated the importance of CD9 in wound re-epithelialization, linking this molecule directly to basement membrane formation and epidermal migration through participating in the regulation of the JNK/MMP-9 pathway. PMID: 21881583
propose that sperm-egg fusion is a direct consequence of CD9 controlled sperm-egg adhesion properties. CD9 generates adhesion sites responsible for the strongest of the observed gamete interaction. PMID: 21690351
knockout mice display abnormal adult angiogenesis PMID: 20592186
This study characterizes CD9 in sperm development and fertilization. PMID: 20428892
Data show that B16F1 lones stably overexpressing CD9 had reduced ability to form colonies in soft agar PMID: 19777564
CD9 is identified as the first receptor for a murine PSG /glycoprotein 17/ PMID: 11805154
role of CD9 in the strengthening of fertilin beta-mediated cell adhesion PMID: 11906941
CD9 may play a role in LIF-mediated maintenance of undifferentiated ES cells. PMID: 11950938
CD9 down-regulation may be a sensitive indicator of macrophage differentiation PMID: 12056820
CD9 inhibits SMC migration by a stimulation of both stress fiber formation and integrin clustering, leading to a stimulation of FAK phosphorylation. PMID: 12083484
the function of CD9 in sperm-egg fusion is was analyzed in CD9-deficient mouse eggs PMID: 12086470
CD9 was enriched in myelinating oligodendrocytes and myelin internodes. Immunoprecipitation of CD9 from postnatal rat cerebrum coprecipitated beta1 integrin, CD81, and Tspan-2. PMID: 12420314
CD9 is found with with the alpha6beta1 integrin heterodimer in parietal endoderm cells , suggesting a role for CD9 in alpha6beta1 mediated migration of parietal endoderm. PMID: 12745436
CD9 is localized to paranodes and has a role in regulating paranodal junctional formation. PMID: 14715942
CD9 is dispensable for B cell development and humoral immunity. PMID: 16116178
During oogenesis the development of the ability of the oolemma to fuse with sperm may be regulated by synthesis of CD9 by the oocyte. PMID: 16719947
Taken together, these results suggest that CD9 expressed on osteoclast lineage cells might positively regulate osteoclastogenesis via the regulation of p44/42 MAPK activity. PMID: 16808899
CD9 expression by multiple myeloma cells is upregulated in vivo by close interaction of the cells with endothelial cells and CD9 is involved in transendothelial invasion PMID: 16900214
CD9 was differentially expressed in uterus depending on the stage of implantation & was upregulated in ovarian steroid hormone-dependent manner, implicating multiple roles of CD9 in regulation of embryo implantation during the peri-implantation period. PMID: 17126340
Oocyte CD9 is enriched on the microvillar membrane and required for normal microvillar shape and distribution. PMID: 17239847
The expression levels of both CD9 mRNA and protein in the frozen oocytes were significantly lower than those found in the fresh oocytes. PMID: 17307168
establish for the first time a role for CD9 in the tumorigenic process PMID: 17582603
The fusion-facilitating activity of CD9-containing vesicles by examining the fusion of sperm to CD9(-/-) eggs with the aid of exogenous CD9-containing vesicles, is investigated. PMID: 18728192
Immunoglobulin superfamily member IgSF8 (EWI-2) and CD9 in fertilisation: evidence of distinct functions for CD9 and a CD9-associated protein in mammalian sperm-egg interaction. PMID: 19210920
macrophage CD9 negatively regulates LPS response at lipid-enriched membrane microdomains PMID: 19414803

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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.