Recombinant Human Spectrin Alpha Chain, Erythrocytic 1 (SPTA1) Protein (His)

Name: Recombinant Human Spectrin Alpha Chain, Erythrocytic 1 (SPTA1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07677P
Price: 349.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins, Recombinant proteins holiday sale

Price Save $1,055

Size

100ug

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Product Overview

Description	Recombinant Human Spectrin Alpha Chain, Erythrocytic 1 (SPTA1) Protein (His) is produced by our Baculovirus expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P02549
Target Symbol	SPTA1
Synonyms	Erythroid alpha-spectrin
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His
Target Protein Sequence	YHLQVFKRDADDLGKWIMEKVNILTDKSYEDPTNIQGKYQKHQSLEAEVQTKSRLMSELEKTREERFTMGHSAHEETKAHIEELRHLWDLLLELTLEKGDQLLRALKFQQYVQECADILEWIGDKEAIATSVELGEDWERTEVLHKKFEDFQVELVAKEGRVVEVNQYANECAEENHPDLPLIQSKQNEVNAAWERLRGLALQRQKALSNAANLQRFKRDVTEAIQWIKEKEPVLTSEDYGKDLVASEGLFHSHKGLERNLAVMSDKVKELCAKAEKLTLSHPSDAPQIQEMKEDLVSSWEHIRALATSRYEKLQATYWYHRFSSDFDELSGWMNEKTAAINADELPTDVAGGEVLLDRHQQHKHEIDSYDDRFQSADETGQDLVNANHEASDEVREKMEILDNNWTALLELWDERHRQYEQ
Expression Range	53-474aa
Protein Length	Partial
Mol. Weight	51.7 kDa
Research Area	Cell
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	Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
Subcellular Location	Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Protein Families	Spectrin family
Database References	HGNC: 11272 OMIM: 130600 KEGG: hsa:6708 STRING: 9606.ENSP00000357130 UniGene: Hs.119825
Associated Diseases	Elliptocytosis 2 (EL2); Hereditary pyropoikilocytosis (HPP); Spherocytosis 3 (SPH3)

Gene Functions References

a novel HE case with a His54Pro mutation in the SPTA1 gene was reported. The results suggested that the His54Pro mutation influenced the role of erythrocyte membrane proteins without reducing its level of expression. PMID: 29484404
A novel SPTA1 mutation (H54P) was identified in a case of hereditary elliptocytosis. PMID: 28694211
The authors show that SUB1-mediated processing of MSP1 is important for parasite viability, the processing modifies the secondary structure of MSP1 and activates its capacity to bind spectrin. PMID: 26468747
The authors demonstrate that the initial vacuolar membrane around internalized Babesia divergens is formed from protein and lipid components of the red blood cells plasma membrane, including band 3, glycophorin A and spectrin. PMID: 25628009
a new function for spectrins in the stability of invadosomes and the coupling between actin regulation and ECM degradation PMID: 25830635
Case Report: severe hemolytic jaundice and a phenotype of hereditary spherocytosis due alpha-spectrin mutations. PMID: 25277063
In this review, we summarize the state of knowledge about interactions between spectrin and membrane lipids PMID: 24569979
A novel exon 2 alpha spectrin mutation is identified in two families of European ancestry with hereditary pyropoikilocytosis. PMID: 24077844
The heterozygous c.121C>T mutation of SPTA1 gene induces an amino acid change p.Arg41Trp in the alpha1 domain of the alpha-spectrin protein. PMID: 24003435
Data show that transcription cofactor TAF3 is required for transcription of the alpha spectrin SPTA1 gene. PMID: 23935956
The common hereditary elliptocytosis-associated alpha-spectrin leucine260proline mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. PMID: 23974198
The unusually slow, two-state kinetics of spectrin assembly in solution, was investigated. PMID: 23200054
In this review, we summarize recent findings concerning structure and function of spectrin together with its possible role in pathology. PMID: 23373410
These data further suggest that residues 44 and 53, which are key players in the nucleation-condensation mechanism of folding, are also important triggers of the aggregation process. PMID: 22727745
analysis of glycosylation of erythrocyte spectrin and its modification in visceral leishmaniasis PMID: 22164239
Further studies involving siRNA-mediated knockdowns of spectrin, adducin, or p4.1 revealed that those proteins are needed for efficient docking of enterohaemorrhagic Escherichia coli to host cells. PMID: 22197999
Results suggest that it is possible for cellular proteins to differentially associate with the C-termini of different beta-spectrin isoforms to regulate alpha- and beta-spectrin association to form functional spectrin tetramers. PMID: 21412925
lipid rafts are associated with the spectrin skeleton in human erythrocytes PMID: 20807499
The data show that the alpha-spectrin EF domain greatly amplifies the function of the beta-spectrin actin-binding domain in forming the spectrin-actin-4.1R complex. PMID: 20585040
The functional roles of residues 21-43 and 55-59 in the alpha-spectrin N-terminal region in forming tetramers were determined;mutations may also introduce abnormalities to erythrocytes. PMID: 19747366
identification and characterization of the gene promoter; requires GATA-1- and NF-E2-binding proteins to direct high level expression in erythroid cells in vitro. PMID: 12196550
Quantitative analysis of erythrocyte membrane proteins revealed increase in alpha-spectrin from patients with homozygous and heterozygous forms of beta-thalassemia. PMID: 15310273
a region 3' of the alpha-spectrin core promoter contains a GATA-1-dependent positive regulatory element that is required in its proper genomic orientation PMID: 15456760
analysis of erythroid alpha and beta spectrin chaperone activity and prodan binding PMID: 15492010
Ubiquitination of alpha-spectrin does not regulate heterodimer formation. PMID: 15795915
splicing mutation in hereditary pyropoikilocytosis kindred PMID: 16150946
We found that cysteine 2071 & cysteine 2100 are critical for alpha-spectrin (2005-2415) E2/E3 activity; also demonstrated that both Cys2071 & Cys2100 are capable of transferring ubiquitin from an E1 enzyme to target sites within alpha-spectrin (2005-2415) PMID: 16171554
the interaction of the alphaII-spectrin SH3 domain with EVL PMID: 16336193
These results suggest a role for spectrin in providing a dynamic and reversible signaling platform to the specific domains of the plasma membrane in response to stimulation of GPCR. PMID: 16551696
Results provide evidence that protein degradation of alphaII-spectrin is a reliable marker of severe traumatic brain injury (TBI) in humans and that both necrotic and apoptotic cell death mechanisms are activated in humans following a severe TBI. PMID: 16841024
REVIEW: Culture studies of Plasmodium falciparum in elliptocytes bearing such elliptocytogenic alleles of spectrin showed that these alleles are supplementary genetic factors of malaria resistance PMID: 17414207
The absence of particular spectrin isoforms may correlate with transformation or aggressive biologic behavior for some lymphoma subtypes. PMID: 17885671
analysis of the conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin PMID: 17905835
This model supports the hypothesis that initial docking of the correct alpha and beta repeats from among many very similar repeats in both subunits is driven primarily by long range electrostatic interactions. PMID: 17977835
All alpha0 HE/HPP mutations studied here appear to exert their destabilizing effects through molecular recognition rather than structural mechanisms. PMID: 18218854
Erythrocytes from most jereditary pyropoikilocytosis (inherited hemolytic anemia) exhibit abnormalities in the alpha-spectrin gene. PMID: 18815189
exon 1' and intron 1' are excellent candidate regions for mutations in patients with spectrin-linked hemolytic anemia PMID: 19008453
The L49F mutation in alpha erythroid spectrin leads to an unstable triple helical bundle of alpha beta-spectrin partial domains, and thus unstable tetramers. PMID: 19593814

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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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