Recombinant Human Platelet Glycoprotein Ib Alpha Chain (GP1BA) Protein (His&Myc)

Name: Recombinant Human Platelet Glycoprotein Ib Alpha Chain (GP1BA) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-08025P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Platelet Glycoprotein Ib Alpha Chain (GP1BA) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P07359
Target Symbol	GP1BA
Synonyms	GP1BA; Platelet glycoprotein Ib alpha chain; GP-Ib alpha; GPIb-alpha; GPIbA; Glycoprotein Ibalpha; Antigen CD42b-alpha; CD antigen CD42b) [Cleaved into: Glycocalicin]
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	SWVGHVKPQALDSGQGAALTTATQTTHLELQRGRQVTVPRAWLLFLRGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGRGQDLLSTVSIRYSGHSL
Expression Range	553-652aa
Protein Length	Partial
Mol. Weight	15.9 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	GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Database References	HGNC: 4439 OMIM: 153670 KEGG: hsa:2811 STRING: 9606.ENSP00000329380 UniGene: Hs.1472
Associated Diseases	Non-arteritic anterior ischemic optic neuropathy (NAION); Bernard-Soulier syndrome (BSS); Bernard-Soulier syndrome A2, autosomal dominant (BSSA2); Pseudo-von Willebrand disease (VWDP)

Gene Functions References

An autosomal dominant mode of inheritance, a family history of mild bleeding episodes, aggregation pattern in affected individuals together with evidence of mutation occurring in part of the GP1BA gene encoding the leucine-rich repeat region suggest a novel variant causing monoallelic Bernard-Soulier syndrome. PMID: 30332551
Combined deficiency of factors V and VIII by chance coinheritance of parahaemophilia and haemophilia A, but not by mutations of either LMAN1 or MCFD2 PMID: 29119711
A review of mutations associated with Bernard-Soulier Syndrome and platelet type von Willebrand disease (review). PMID: 28961024
ERK5 associates with CKII to play essential roles in GPIb-IX-mediated platelet activation via the PTEN/PI3K/Akt pathway. PMID: 28603902
There was no evidence to suggest that polymorphisms of GP VI T13254C and GP Ibalpha VNTR were associated with CAD. PMID: 28607925
analysis of an artificial botrocetin that can inhibit the VWF-GPIb interaction PMID: 28071872
Loss of the platelet surface receptors GPIbalpha and GPVI in heart failure, CF-VAD and ECMO patients may contribute to ablated platelet adhesion/activation, and limit thrombus formation under high/pathologic shear conditions PMID: 27601054
Very low birth weight preterm neonates have increased numbers of platelets interacting with von Willebrand Factor, and increased GPIbalpha expression on the platelet surface PMID: 27416003
Data suggest that an aspartate at position 1261 is the most critical residue of VWF N-terminal linker for inhibiting binding of VWF A1 domain to GP1BA on platelets in a model simulating blood flow velocity; network of salt bridges between Asp1261 and rest of VWF A1 domain lock N-terminal linker in place such that binding to GP1BA is reduced. PMID: 28924049
Data show that von Willebrand factor (VWF) is first converted from a compact to linear form by flow, and is subsequently activated to bind platelet glycoprotein Ib alpha polypeptide (GPIbalpha) in a tension-dependent manner. PMID: 28831047
The >30 nm macroglycopeptide separating the two domains of GPIbalpha transmits force on the VWF-GPIbalpha bond (whose lifetime is prolonged by leucine-rich repeat domain unfolding) to the juxtamembrane mechanosensitive domain to enhance its unfolding, resulting in unfolding cooperativity at an optimal force. PMID: 27434669
Meta-analysis found that glycoprotein Ia C807T T allele or the TT genotype, the Ser-allele of HPA-3 and B allele of glycoprotein Ibalpha variable number tandem repeat polymorphisms were associated with increased risk for ischemic stroke. PMID: 28004990
Our results suggest that the -5CC genotype in Kozak sequence of GPIb-alpha may be associated with a higher risk of developing arterial ischemia of lower limbs in type 2 diabetes mellitus patients. PMID: 27888791
Specific inhibition of GPIbalpha shedding in the stored platelets improves post-transfusion platelet recovery and hemostatic function, providing clear evidence for GPIbalpha shedding as a cause of platelet clearance. PMID: 27417583
miR-10a and miR10b regulate the expression of human platelet GP1BA and GP1bb for normal megakaryopoiesis. PMID: 27834869
Data indicate that binding of hemoblobin (Hb) to glycoprotein1balpha (GP1balpha) induced platelet activation plays a crucial role in thrombus formation on immobilized von Willebrand factor (VWF) or type I collagen under shear stresses. PMID: 27105433
Lateral dimerization of GPIbalpha induced by antibody binding is not sufficient to initiate GPIb-IX signaling and induce platelet clearance. PMID: 26662889
GPIb alpha plays a critical role in the co-localization of thrombin and factor XI and the resultant efficient activation of FXI PMID: 12968031
Hemoglobin interaction with GP1balpha induces platelet activation and apoptosis: a novel mechanism associated with intravascular hemolysis. PMID: 26341739
Both GPIbalpha and PAR4 are required for thrombin-induced reactive oxygen species formation PMID: 26569550
Our results reveal the molecular mechanism of collagen-regulated, A1-mediated platelet adhesion enhancement. PMID: 26213126
Report no relationship, between polymorphisms of platelet membrane glycoprotein Ibalpha and risk of coronary heart disease in Chinese Han population. PMID: 26191334
There is a prevalence of Thr145Met and T(-5)C GP Iba polymorphiams in patients with atherotrombotic stroke due to macroangiopathy. PMID: 26539867
Molecular analysis demonstrated a novel homozygous c.800C>G substitution in GP1BA exon 2 leading to a serine 267 Ter stop codon in all 3 siblings PMID: 26044173
Whereas VWF-D'D3 is the major regulator of soluble VWF binding to platelet GpIbalpha, both the D'D3-domain and N-terminal peptide regulate platelet translocation and thrombus formation. PMID: 25341886
Data indicate that GPIbalpha clustering induced by anti-GPIbalpha N-terminus antibody causes integrin alphaIIbbeta3-dependent platelet aggregation, phagocytosis, and rapid platelet clearance in the liver. PMID: 25231551
Data show that force can switch the kinetics of bond formation between A1 domain of von Willebrand factor (VWF) and glycoprotein Ibalpha (GPIbalpha). PMID: 25810255
novel mutation that causes von Willebrand disease type 2B is identified in a German family PMID: 24337418
The platelet adhesion receptor, the glycoprotein Ib-IX-V complex, not only mediates platelet adhesion but also transmits signals leading to platelet activation, aggregation and secretion PMID: 17414217
data indicated that GPIIb-IIIa and GPIb levels are mainly affected by platelet size (MPV) but not by their genetic variations; in some acute coronary syndrome patients, production of large platelets with high GPIIb-IIIa and GPIb contents might be stimulated by elevated thrombopoietin PMID: 23941967
Data indicate a G > T in platelet glycoprotein Ib alpha polypeptide (GP1BA) gene, resulting in a Trp to Leu amino acid change at residue 246 (p.W246L), and this mutation was absent in his unaffected mother and also in the 100 controls. PMID: 24474090
clone 5G6 showed similar inhibitory potency as a widely used shedding inhibitor GM6001 in both constitutive and induced GPIbalpha shedding in human platelets PMID: 24119228
VWF interaction with glycoprotein Ib is modified by polyphosphate PMID: 23006049
Our findings indicate that ADAM17 may be a risk factor for ischemic stroke in Chinese and the expression of GPIbalpha can serve as a measure for stroke severity. PMID: 23771674
Platelet GP Ib-IX can be considered a multifunctional participant in hemostasis, thrombosis, and the inflammatory cascade. PMID: 24504734
Increased mean platelet volume values correlated with increased platelet aggregation activity and enhanced GP IIb-IIIa and GP Ib expression. PMID: 24749250
These findings suggest that structural changes, including central GPIbalpha LRR-A1 contact, contribute to VWF affinity regulation. PMID: 24391089
genetic association study in population in western India: Data suggest novel mutations in platelet glycoprotein Ib (GP1BA, GP1BB) and GP9 are associated with Bernard-Soulier syndrome in subjects studies; of 12 mutations identified, ten were novel. PMID: 23995613
Studies indicate that the platelet-type von Willebrand disease (PT-VWD) is caused by gain-of-function mutations in the platelet GP1BA gene, which codes for the platelet von Willebrand factor (VWF) receptor, GPIbalpha. PMID: 23934752
Studies indicate that platelets from Bernard-Soulier syndrome (BSS) are defective in glycoprotein (GP)Ib-IX-V, a platelet-specific adhesion-signaling complex, composed of GPIbalpha disulfide linked to GPIbbeta, and noncovalently associated with GPIX and GPV. PMID: 23929303
signaling process through the GPIbalpha cytoplasmic tail required for full platelet activation is defective in BSS variant case II and a length polymorphism of GPIbalpha is associated with a modified level of RIPA heterozygous BSS case I. PMID: 23414566
analysis of the localized dynamics-driven affinity regulation mechanism for vWF-GPIbalpha interaction PMID: 23902764
These data indicate an important role for the platelet adhesion receptor GPIb-IX in endotoxin-induced thrombosis and thrombocytopenia. PMID: 24051142
A considerable fraction of the Jordanian population is resistant to the antiplatelet effect of aspirin, which might be related to GPIba C-5T polymorphism. PMID: 23688555
A GP1BA exon 2 fragment spanned the HPA-2 polymorphism and adjacent sequences. PMID: 23750933
genotype may predict the development of septic emboli in patients with infective endocarditis PMID: 23611001
identify a novel Asp235Tyrmutation in the GP1BA gene of two Iranian patients showing the PT-VWD phenotype who were originally misdiagnosed as type 2B VWD PMID: 23014764
GPIX increased the expression of GPIba by promoting the formation of a disulfide bond between GPIba and GPIbb in transfected CHO-K1 cells. PMID: 23143686
Data indicate that exposure of von Willebrand factor sites for glycoprotein Ibalpha binding and ADAMTS13 cleavage are coupled. PMID: 22922961
The T1255A, Clus1, and DC variants caused increased ristocetin-mediated GPIbalpha binding to VWF. PMID: 22517896

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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.

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