Analytical Data
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Gene name
SH3BP5L
- Application
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Alternative Names
SH3BP5L; KIAA1720; UNQ2766/PRO7133SH3 domain-binding protein 5-like; SH3BP-5-like
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q7L8J4
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Expression Region
1-393 aa
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AA Sequence
MAELRQVPGG RETPQGELRP EVVEDEVPRS PVAEEPGGGG SSSSEAKLSP REEEELDPRI QEELEHLNQA SEEINQVELQ LDEARTTYRR ILQESARKLN TQGSHLGSCI EKARPYYEAR RLAKEAQQET QKAALRYERA VSMHNAAREM VFVAEQGVMA DKNRLDPTWQ EMLNHATCKV NEAEEERLRG EREHQRVTRL CQQAEARVQA LQKTLRRAIG KSRPYFELKA QFSQILEEHK AKVTELEQQV AQAKTRYSVA LRNLEQISEQ IHARRRGGLP PHPLGPRRSS PVGAEAGPED MEDGDSGIEG AEGAGLEEGS SLGPGPAPDT DTLSLLSLRT VASDLQKCDS VEHLRGLSDH VSLDGQELGT RSGGRRGSDG GARGGRHQRS VSL
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Molecular Weight
43.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SH3BP5L, a protein belonging to the SH3 domain-binding protein family, has garnered attention in recent years due to its potential roles in cellular processes such as signal transduction, endocytosis, and cytoskeletal organization. Research indicates that SH3BP5L interacts with various proteins involved in these pathways, suggesting its significance in regulating cellular responses to external stimuli. Dysregulation of SH3BP5L has been implicated in various diseases, including cancer, where it may influence tumor progression and metastasis by affecting cellular signaling networks. Moreover, understanding the functional dynamics of SH3BP5L and its interaction partners can provide insights into novel therapeutic targets. The recombinant expression of SH3BP5L allows for detailed biochemical and structural studies, enabling researchers to dissect its mechanisms of action and explore its potential as a biomarker or therapeutic target in disease contexts. By elucidating the pathways and interactions involving SH3BP5L, scientists aim to uncover fundamental biological processes and develop strategies for disease intervention, making it a focus of current protein research.
