Product Description

Recombinant Human ADP-Ribosylation Factor-Like 6 (ARL6) is a protein that belongs to the ADP-ribosylation factor (ARF) family. With a molecular weight of approximately 21 kDa, ARL6 plays a role in intracellular vesicular trafficking and protein transport. It is involved in the regulation of cilia formation and maintenance, making it a crucial component in cellular processes. Understanding the functions and characteristics of ARL6 is vital for comprehending its implications in various physiological and pathological conditions.

Current Lead Time

7-14 Days

Product Specifications

*For Research Use Only

If your product is within its expiration period, and has not performed according to expectations, fill out the sample return form. Return the unused sample frozen, with the auto generated packing slip to the address on the instructions. You will receive a full refund along with a replacement of the unused portion (inclusive of the failed test). Damages do not cover any additional costs incurred for failed experimentation. 

MGSSHHHHHH SSGLVPRGSH MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ IQTVKT.

Reconstituted store at -20°C or -80°C.We recommend that single use aliquots are prepared to avoid freeze-thaw cycles.

1. Thaw the vial on ice, spin briefly
2. Prepare single-use or stock aliquots. This stage will depend on your final application so please adapt as appropriate. All our proteins are supplied carrier protein-free. If compatible with your work and you are storing at lower concentrations (<50 ug/ml) adding carrier protein is highly advised (usually 1% w/v high purity BSA or equivalent – ensure all buffers are sterile-filtered).
3. Prepare single-use aliquots whenever possible to avoid freeze-thaw cycles which can damage the proteins and reduce bioactivity. Store aliquots at -70 °C (or -20 °C)
4. We recommend sterile filtering after dilution in media or the final working solution
​

Not Available