Recombinant Human Brca1-Associated Protein (BRAP) Protein (His)

Name: Recombinant Human Brca1-Associated Protein (BRAP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06684P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Brca1-Associated Protein (BRAP) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q7Z569
Target Symbol	BRAP
Synonyms	(BRAP2)(Impedes mitogenic signal propagation)(IMP)(RING finger protein 52)(RING-type E3 ubiquitin transferase BRAP2)(Renal carcinoma antigen NY-REN-63)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	SVSLVVIRLELAEHSPVPAGFGFSAAAGEMSDEEIKKTTLASAVACLEGKSPGEKVAIIHQHLGRREMTDVIIETMKGGGGSGGGGSEIVHGIMHLYKTNKMTSLKEDVRRSAMLCILTVPAAMTSHDLMKFVAPFNEVIEQMKIIRDSTPNQYMVLIKFRAQADADSFYMTCNGRQFNSIEDDVCQLVYVERAEVLKSEDGASLPVMDLTELPLE
Expression Range	2-262aa
Protein Length	Partial
Mol. Weight	24.5 kDa
Research Area	Epigenetics And Nuclear Signaling
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	Negatively regulates MAP kinase activation by limiting the formation of Raf/MEK complexes probably by inactivation of the KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase that, on activation of Ras, is modified by auto-polyubiquitination resulting in the release of inhibition of Raf/MEK complex formation. May also act as a cytoplasmic retention protein with a role in regulating nuclear transport.
Subcellular Location	Cytoplasm.
Database References	HGNC: 1099 OMIM: 604986 KEGG: hsa:8315 STRING: 9606.ENSP00000403524 UniGene: PMID: 28562329 IMPACT data were consistent with increased risks of onset among BRCA1 and BRCA2 mutation carriers PMID: 27742670 Expression of BRAP is increased in esophageal squamous cell carcinoma samples compared with non-tumor esophageal tissues; increased expression correlates with reduced patient survival time and promotes metastasis of xenograft tumors in mice. PMID: 28780075 Together the results indicate for the first time that BRAP2 may play an important NRNI role in germ cells of the testis, with an additional, scaffold/structural role in mature spermatozoa. PMID: 25820252 BRAP gene may confer vulnerability for schizophrenia in Han Chinese population. PMID: 24454952 ectopic expression of BRAP2 inhibits nuclear localization of HMG20A and NuMA1, and prevents nuclear envelope accumulation of SYNE2. PMID: 23707952 genetic association studies in population of Chinese Han young adults in Beijing: Data suggest that 2 SNPs in BRAP (rs11066001; rs3782886) are associated with decreased risk of metabolic syndrome in this population. PMID: 22965072 BAP1 expression closely correlates with age, clinical stage, pathologic differentiation and histological type in colorectal cancer (CRC). BAP1 may serve as a novel prognostic biomarker for CRC. PMID: 23526420 Brap2 regulates temporal control of NF-kappaB localization mediated by inflammatory response. PMID: 23554956 The BRAP polymorphism may not play an important role in ischemic stroke in the Taiwanese population. PMID: 23356535 The dominant effect of prolonged USP15 depletion upon signal amplitude is due to a decrease in CRAF levels while allowing for the possibility that USP15 may also function to dampen MAPK signaling through direct stabilization of BRAP. PMID: 23105109 ANRIL on 9p21 and BRAP were both associated with ankle brachial index in a Taiwanese population. PMID: 22122968 Several BRCA1 mutations were observed in Pakistani breast cancer patients with moderate family history. PMID: 22078348 Data show that BRAP conferred a risk for carotid plaque and intima-medial thickness. PMID: 21670849 BRAP gene is associated with the extent of coronary atherosclerosis and has a synergistic effect with diabetes on the occurrence of significant CAD in the Chinese population PMID: 22085839 our approach, which is applicable to any set of interval scale traits that is heritable and exhibits evidence of phenotypic clustering, identified three new loci in or near APOC1, BRAP, and PLCG1, which were associated with multiple phenotype domains. PMID: 22022282 Polymorphism of 270 A > G in BRAP is Associated with Lower Ankle-Brachial Index and peripheral artery disease. PMID: 21301165 All results are consistent with BRAP2 being a novel, phosphorylation-regulated negative regulator of nuclear import, with potential as an antiviral agent. PMID: 20040518 Data indicate that one SNP in BRAP showed(rs11066001) a significant association in allele frequency distribution with CAD in both the Japanese and Korean populations. PMID: 19713974 modulates sensitivity of the MAP kinase cascade to stimulus-dependent activation by limiting functional assembly of the core enzymatic components through the inactivation of KSR PMID: 14724641 Monocytic differentiation of the promyelomonocytic cell lines U937 and HL60 is associated with the upregulation of Brap2 expression concomitantly with the upregulation and cytoplasmic relocalization of p21. PMID: 15340083 the capacity of IMP to inhibit signal propagation through Raf to MEK is a consequence of disrupting KSR1 homooligomerization and B-Raf/c-Raf hetero-oligomerization PMID: 18332145 The most current evidence suggests that it may be more beneficial in those with BRCA mutations because tumors associated with these mutations are likely to be estrogen-receptor positive. PMID: 18380995 p21 Ras/Imp regulate cytokine production and migration in CD4 T cells [Imp] PMID: 18577512 Carriers of mutations in the genes BRCA1/2 may present a specific high risk group for PABC especially at younger ages. PMID: 19009954 The authors found that Brap2, which has intrinsic RING domain dependent E3 ligase activity, facilitates HsCdc14A Lys-63 linked ubiquitin modification, indicating that Brap2 may be the ubiquitin E3 Ligase of HsCdc14A. PMID: 19152073 SNPs in BRAP associated with risk of myocardial infarction in Asian populations.BRAP knockdown in cultured coronary endothelial cells suppressed activation of NF-kappaB. PMID: 19198608

FAQs

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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.