Recombinant Human Spectrin Alpha Chain, Non-Erythrocytic 1 (SPTAN1) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04124P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Spectrin Alpha Chain, Non-Erythrocytic 1 (SPTAN1) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04124P
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Product Overview

Description Recombinant Human Spectrin Alpha Chain, Non-Erythrocytic 1 (SPTAN1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q13813
Target Symbol SPTAN1
Synonyms (ALPHA)II-SPECTRIN; Alpha II Spectrin; Alpha-II spectrin; brain; EIEE5; FLJ17738; FLJ44613; Fodrin alpha chain; Fodrin, alpha; NEAS; Non erythrocytic spectrin alpha; non-erythroid alpha chain; SPECA; Spectrin alpha chain; Spectrin alpha chain brain; Spectrin alpha non erythrocytic 1; Spectrin; Spectrin non erythroid alpha chain; Spectrin, alpha, non-erythrocytic 1 (alpha-fodrin); Spectrin, nonerythroid, alpha subunit; Spna2; SPTA 2; SPTA2; SPTA2_HUMAN; SPTAN 1; SPTAN1
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MDPSGVKVLETAEDIQERRQQVLDRYHRFKELSTLRRQKLEDSYRFQFFQRDAEELEKWIQEKLQIASDENYKDPTNLQGKLQKHQAFEAEVQANSGAIVKLDETGNLMISEGHFASETIRTRLMELHRQWELLLEKMREKGIKLLQAQKLVQYLRECEDVMDWINDKEAIVTSEELGQDLEHVEVLQKKFEEFQTDMAAHEERVNEVNQFAAKLIQEQHPEEELIKTKQDEVNAAWQRLKGLALQRQGKLFGAAEVQRFNRDVDETISWIKEKEQLMASDDFGRDLASVQALLRKHEGLERDLAALEDKVKALCAEADRLQQSHPLSATQIQVKREELITNWEQIRTLAAERHARLNDSYRLQRFLADFRDLTSWVTEMKALINADELASDVAGAEALLDRHQEHKGEIDAHEDSFKSADESGQALLAAGHYASDEVREKLTVLSEERAALLELWELRRQQYEQCMDLQLFYRDTEQVDNWMSKQEAFLLNEDLGDSLDSVEALLKKHEDFEKSLSAQEEKITALDEFATKLIQNNHYAMEDVATRRDALLSRRNALHERAMRRRAQLADSFHLQQFFR
Expression Range 1-580aa
Protein Length Partial
Mol. Weight 83.8kDa
Research Area Signal Transduction
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 Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.
Subcellular Location Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Protein Families Spectrin family
Database References

HGNC: 11273

OMIM: 182810

KEGG: hsa:6709

STRING: 9606.ENSP00000361824

UniGene: PMID: 29244882

  • SPTAN1-related disorders comprise a wide spectrum of neurodevelopmental phenotypes ranging from mild to severe and progressive. Spectrin aggregate formation in fibroblasts with mutations in the alpha/beta heterodimerization domain seems to be associated with a severe neurodegenerative course. PMID: 29050398
  • Alpha-spectrin is critical for recruitment of non-ubiquitinated FANCD2 to sites of damage, which has an important role in the repair response and interstrand cross-link repair. PMID: 26297932
  • Studies demonstrate that alpha-IISp plays a critical role in maintaining chromosome stability in cells after DNA interstrand cross-links damage by repairing damage that occurs in both genomic and telomeric DNA. PMID: 25757157
  • These results suggest that ubiquitin C-terminal hydrolase and alphaII-spectrin breakdown product 145 kDa may be useful in assessing outcome after pediatric traumatic brain injury. PMID: 22022780
  • Variations in both alpha-spectrin (SPTA1) and beta-spectrin ( SPTB ) were found in a neonate with prolonged jaundice in a family where nine individuals had hereditary elliptocytosis. PMID: 24193021
  • aggressiveness of MLH1-positive colorectal cancers might be related to SPTAN1. PMID: 24456667
  • hypomyelination of the cerebral white matter was revealed at the age of 1 year, and a de novo heterozygous mutation in the SPTAN1 gene was confirmed PMID: 22656320
  • loss of SPTAN1 switches TGF-beta signaling from tumor suppression to tumor promotion by engaging Notch signaling and activating SOX9 in esophageal adenocarcinoma. PMID: 23536563
  • organization of a spectrin-like cytoskeleton is associated with keratinocyte differentiation, and cytoskeleton disruption is mediated by either PKCdelta(Thr505) phosphorylation associated with phosphorylated adducin or due to reduction of endogenous adducin PMID: 22163289
  • In-frame mutations in the C-terminus of SPTAN1 cause a core set of manifestations that include severe intellectual disability, generalized epilepsy, and pontocerebellar atrophy. PMID: 22258530
  • Analysis of alphaII-spectrin breakdown products in cerebrospinal fluid predicts mortality and injury severity in adults following traumatic brain injury. PMID: 20408766
  • findings suggest that pathological aggregation of alpha/beta spectrin heterodimers and abnormal axon initial segment(AIS) integrity resulting from SPTAN1 mutations were involved in pathogenesis of infantile epilepsy PMID: 20493457
  • Fanconi anemia proteins may play an important role in maintaining the stability of alphaIISp in the cell by regulating its cleavage by mu-calpain. PMID: 20518497
  • This protein has been found differentially expressed in the anterior cingulate cortex from patients with schizophrenia PMID: 20381070
  • SigA binds to epithelial HEp-2 cells as well as being able to induce fodrin degradation in vitro and in situ, further extending its documented role in the pathogenesis of Shigella infections. PMID: 20011051
  • Review. 120 kDa alpha-fodrin is an important autoantigen in both animal models and Sjogren syndrome patients. Increased caspase cascade activity may be involved in the progression of alpha-fodrin proteolysis and tissue destruction. PMID: 12630566
  • High affinity and slow overall kinetics of association/dissociation of alpha II-spectrin may suit it well to a role in strengthening cell junctions and providing stable anchorage for transmembrane proteins at points specified by cell-adhesion molecules. PMID: 12820899
  • Fanconi anemia cell lines deficient in alphaII spectrin express normal levels of alphaII spectrin mRNA. PMID: 12893251
  • These observations indicate that calpain is activated and reacts with alpha-fodrin as a substrate at the sarcolemma, and plays a key role in modulating sarcolemmal proteins to adapt to the specific conditions in each myopathy. PMID: 15948206
  • The in vivo role of alpha-fodrin autoantigen in primary Sjogren's syndrome was analyzed. PMID: 16192640
  • These studies indicate that alphaSpIISigma( *) may play a role in a number of diverse and important processes in the nucleus and that a deficiency in this protein, as occurs in Fanconi's anemia, could affect a number of critical cellular pathways. PMID: 16889989
  • provide novel insights into spectrin functions by demonstrating the involvement of alphaII-spectrin in cell cycle regulation and actin organization PMID: 18978357
  • The SH3 domain of SPTAN1 is a target for the Fanconi anemia protein, FANCG. PMID: 19102630
  • depletion of alphaIISp in normal cells leads to a number of defects observed in Fanconi anemia cells, such as chromosome instability and a deficiency in cross-link repair. PMID: 19217883
  • fodrin degradation occurs during galectin-1 T cell death and CD45 is essential for fodrin degradation to occur PMID: 19454697
  • This protein has been found differentially expressed in the temporal lobe from patients with schizophrenia. PMID: 19034380
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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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