Recombinant Mouse Gdnf Family Receptor Alpha-1 (GFRA1) Protein (His)

Name: Recombinant Mouse Gdnf Family Receptor Alpha-1 (GFRA1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04885P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Gdnf Family Receptor Alpha-1 (GFRA1) Protein (His) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P97785
Target Symbol	GFRA1
Synonyms	Gfra1; Gdnfra; Trnr1; GDNF family receptor alpha-1; GDNF receptor alpha-1; GDNFR-alpha-1; GFR-alpha-1; TGF-beta-related neurotrophic factor receptor 1
Species	Mus musculus (Mouse)
Expression System	Baculovirus
Tag	C-6His
Target Protein Sequence	DRLDCVKASDQCLKEQSCSTKYRTLRQCVAGKETNFSLTSGLEAKDECRSAMEALKQKSLYNCRCKRGMKKEKNCLRIYWSMYQSLQGNDLLEDSPYEPVNSRLSDIFRAVPFISDVFQQVEHISKGNNCLDAAKACNLDDTCKKYRSAYITPCTTSMSNEVCNRRKCHKALRQFFDKVPAKHSYGMLFCSCRDVACTERRRQTIVPVCSYEERERPNCLNLQDSCKTNYICRSRLADFFTNCQPESRSVSNCLKENYADCLLAYSGLIGTVMTPNYIDSSSLSVAPWCDCSNSGNDLEDCLKFLNFFKDNTCLKNAIQAFGNGSDVTMWQPAPPVQTTTATTTTAFRIKNKPLGPAGSENEIPTHVLPPCANLQAQKLKSNVSGSTHLCLSDNDYGKDGLAGASS
Expression Range	25-430aa
Protein Length	Full Length of Mature Protein
Mol. Weight	46.5
Research Area	Neuroscience
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.
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	Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor.
Subcellular Location	Cell membrane; Lipid-anchor, GPI-anchor. Golgi apparatus, trans-Golgi network. Endosome. Endosome, multivesicular body.
Protein Families	GDNFR family
Database References	KEGG: mmu:14585 STRING: 10090.ENSMUSP00000026076 UniGene: PMID: 29339164 Compromised Survival of Cerebellar Molecular Layer Interneurons Lacking GDNF Receptors GFRalpha1 or RET Impairs Normal Cerebellar Motor Learning. PMID: 28591570 GFRA1 regulates AMPK-dependent autophagy by promoting SRC phosphorylation independent of proto-oncogene RET kinase PMID: 27754745 the neural cell adhesion molecule NCAM is co-expressed and directly interacts with GFRalpha1 in embryonic Purkinje cells. PMID: 28076782 LncRNA033862 is an antisense transcript of the GDNF receptor alpha1 (Gfra1) that lacks protein coding potential and regulates Gfra1 expression levels by interacting with Gfra1 chromatin. PMID: 26962690 These findings collectively demonstrate that GFRalpha1 released by nerves enhances perineural invasion through GDNF-RET signaling and that GFRalpha1 expression by cancer cells enhances but is not required for it. PMID: 24778213 Gfra1 expression in the urinary tract strictly depends on cell-type and specific stage in kidney development. PMID: 23542432 our data demonstrate that RET/GFRalpha signals are dispensable for thymic T cell development in vivo PMID: 23300832 GFRalpha1 is critical for the development and function of the main olfactory system, contributing to the development and allocation of all major classes of neurons and glial cells. PMID: 23197722 Donor-derived GFRalpha1-positive cells formed several aggregates of A(al(aligned)) /morula-like structures in a single spermatogenic cell patch before and on day 14 post-transplant, indicating involvement in the formation of a stable spermatogenic colony. PMID: 22745058 GFRA1 expression is regulated by GDNF and in cultures of isolated seminiferous tubules, we found that GDNF expression and secretion by Sertoli cells is stage-dependent, being maximal in stages II-VI and decreasing thereafter. PMID: 22143971 Histone methylation and acetylation regulate Pou5f1 and Gfra1 in male germ cell. PMID: 20856864 Following ischemic injury, GFR alpha-1 is differentially up-regulated in GFR alpha-1 (+/+) and GFR alpha-1 (+/-) mice. PMID: 12697293 localization pattern of c-kit, Notch-1 and GFRalpha-1 in postnatal, immature and adult testes PMID: 15237212 GFR alpha-1, the receptor for GDNF is strongly expressed by a subset of type A spermatogonia. PMID: 15708562 The role of GFRalpha1 in the developing brain is to promote the differentiation and migration of cortical GABAergic neurons. PMID: 15748846 Data suggest that the combinatorial interactions of the spliced isoforms of GFRalpha, RET and NCAM may contribute to the pleiotropic biological responses. PMID: 15979200 Spermatogonial stem cells expresses GFRA1, but also the stem cell pool is heterogeneous with respect to the level of GFRA1 expression PMID: 16014811 Conditional ablation of GFRalpha1 in postmigratory enteric neurons triggers unconventional neuronal death in the colon and causes a Hirschsprung's disease phenotype. PMID: 17507417 Gfra1 is expressed dominantly in mouse spermatogonial stem cells; Gfra1 knockdown leads to their differentiation via the inactivation of RET tyrosine kinase, suggesting an essential role for Gfra1 in spermatogonial stem cell regulation. PMID: 17625109 The absence of Gfr alpha1 had no effect on either the appearance of brain-derived fatty acid binding protein (B-FABP) cells or the relative area of the ganglia occupied by B-FABP-immunoreactive cells. PMID: 18551627 The findings point to increased sensitivity of the DAergic system with age and neurotoxic exposure as a result of a genetic reduction of GFR alpha1. PMID: 18822276 The present study clearly establishes that genetic reductions in GFRalpha-1 can contribute to the degenerative changes observed in this system during the aging process. PMID: 18973577 From the data of this study suggested that GFR1 signaling guides the development of a subset of parvalbumin-expressing GABAergic interneurons populating discrete regions of the cerebral cortex. PMID: 19710321

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.