Recombinant Human Atpase Asna1 (ASNA1) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-09918P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Atpase Asna1 (ASNA1) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-09918P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Atpase Asna1 (ASNA1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O43681
Target Symbol ASNA1
Synonyms ARSA 1; ARSA; ArsA arsenite transporter ATP binding homolog 1; ArsA arsenite transporter; ATP binding; E. coli; homolog of; 1; ArsA arsenite transporter; ATP-binding; homolog 1 (bacterial); ARSA I; ARSA-I; ARSA1; ARSAI; Arsenical pump driving ATPase; Arsenical pump-driving ATPase; Arsenical resistance ATPase; Arsenite translocating ATPase; Arsenite transporting ATPase; Arsenite-stimulated ATPase; ASNA 1; ASNA I; ASNA-I; ASNA_HUMAN; ASNA1; Asna1 protein ; ASNAI; ATPase ASNA1; GET3; Golgi to ER traffic 3 homolog; hARSA-I; hASNA-I; MGC3821; Transmembrane domain recognition complex 40 kDa ATPase subunit; Transmembrane domain recognition complex; 40kDa; TRC40
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence AAGVAGWGVEAEEFEDAPDVEPLEPTLSNIIEQRSLKWIFVGGKGGVGKTTCSCSLAVQLSKGRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCKIDTHNIIVNQLVFPDPEKPCKMCEARHKIQAKYLDQMEDLYEDFHIVKLPLLPHEVRGADKVNTFSALLLEPYKPPSAQ
Expression Range 2-348aa
Protein Length Full Length of Mature Protein
Mol. Weight 54.7kDa
Research Area Transport
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 ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-CAMLG receptor, and returning it to the cytosol to initiate a new round of targeting. May be involved in insulin signaling.
Subcellular Location Cytoplasm. Endoplasmic reticulum. Nucleus, nucleolus.
Protein Families ArsA ATPase family
Database References
Tissue Specificity Expressed in the epithelial cells of the liver, kidney, and stomach wall, in the adrenal medulla, in the islet cells of the pancreas, in the red pulp of the spleen, and in cardiac and skeletal muscle.

Gene Functions References

  1. The authors conclude that the TRC40 pathway is critical for hearing and propose that otoferlin is an essential substrate of this pathway in hair cells. PMID: 27458190
  2. Asna1/TRC40 is required at a late step of herpes simplex virus type 1 infection for efficient release of mature virions to the extracellular milieu. PMID: 27765046
  3. reveal unanticipated complexity in the mutual regulation of the TRC40 receptor subunits and raise the question as to the role of the excess CAML in the endoplasmic reticulum PMID: 27226539
  4. Emerin interacts with TRC40 in situ. PMID: 26675233
  5. The repertoire of VAPB interactors is more diverse than previously anticipated and link VAPB to the function of ATPase complexes such as p97/FAF1 and ASNA1/transmembrane-domain recognition complex. PMID: 24885147
  6. Proteins bind to TRC40 and can utilise this component for their delivery to the ER membrane. PMID: 22505607
  7. PEX19 formed a complex with the peroxisomal tail anchored protein PEX26 in the cytosol and translocated it directly to peroxisomes by a TRC40-independent class I pathway. PMID: 23460677
  8. Results indicate calcium-modulating cyclophilin ligand (CAML) and WRB as components of the TRC40 receptor complex and a crucial mechanism for driving ER membrane insertion of TA proteins in mammalian cells. PMID: 23041287
  9. Post-translational membrane insertion of tail-anchored transmembrane EF-hand Ca2+ sensor calneurons requires the TRC40/Asna1 protein chaperone. PMID: 21878631
  10. The coiled-coil domain of WRB is the binding site for TRC40/Asna1. PMID: 21444755
  11. Asna1 is required for efficient histocompatibility (HLA) class I downregulation mediated by viral protein BNLF2a. PMID: 21296983
  12. Asna1 can mediate membrane insertion of RAMP4 and Sec61beta without the participation of other cytosolic proteins by a mechanism that depends on the presence of ATP or ADP and a protease-sensitive receptor in the endoplasmic reticulum membrane. PMID: 20375064
  13. Human ASNA1 is highly expressed in pancreatic beta cells, but not in other pancreatic endocrine cell types, and regulates insulin secretion in cultured cells. PMID: 17289575
  14. TRC40/Asna-1 interacts posttranslationally with tail-anchored proteins in a transmembrane domain-dependent manner for delivery to a proteinaceous receptor at the endoplasmic reticulum membrane. PMID: 17382883
  15. the hydrophobicity of the TA region dictates whether a precursor is delivered to the ER via the Hsp40/Hsc70 or Asna-1/TRC40-dependent route. PMID: 18667436
  16. ASNA1 is a target to overcome platinum resistance in ovarian cancer PMID: 19724867

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.

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