Analytical Data
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Gene name
SLA
- Application
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Alternative Names
hSLAP; SLA 1; sla; SLA1; SLAP 1; SLAP; SLAP-1; SLAP1; SLAP1_HUMAN; Src like adapter; Src like adapter protein 1; Src like adaptor; SRC-like-adapter; Src-like-adapter protein 1
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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
Q13239
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Expression Region
2-276 aa
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AA Sequence
GNSMKSTPA PAERPLPNPE GLDSDFLAVL SDYPSPDISP PIFRRGEKLR VISDEGGWWK AISLSTGRES YIPGICVARV YHGWLFEGLG RDKAEELLQL PDTKVGSFMI RESETKKGFY SLSVRHRQVK HYRIFRLPNN WYYISPRLTF QCLEDLVNHY SEVADGLCCV LTTPCLTQST AAPAVRASSS PVTLRQKTVD WRRVSRLQED PEGTENPLGV DESLFSYGLR ESIASYLSLT SEDNTSFDRK KKSISLMYGG SKRKSSFFSS PPYFED
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Molecular Weight
31.1 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
SLA (Streptolysin S-like) reorganized proteins have garnered significant attention in recent years due to their unique structural and functional characteristics. These proteins are primarily produced by certain bacterial species and play key roles in pathogenesis, particularly in evading host immune responses. The understanding of SLA proteins has been propelled by advancements in molecular biology and structural biology techniques, allowing researchers to unveil their intricate mechanisms and interactions at the molecular level. Furthermore, the potential of these proteins in therapeutic applications, such as vaccine development and targeted drug delivery, has spurred extensive research efforts. Studies have highlighted how SLA proteins modulate cellular pathways and influence host marker expression, making them critical for understanding bacterial virulence and host-pathogen interactions. As such, the exploration of SLA restructured proteins promises not only to enhance our understanding of bacterial biology but also to provide valuable insights into the development of novel therapeutic strategies for infectious diseases.
