Alternative Name(s):

rpsS; b3316; JW3278; 30S ribosomal protein S19; Small ribosomal subunit protein uS19

Species: (Organism)

Escherichia coli (strain K12)

Gene Names:

rpsS

Tag info:

N-terminal 6xHis-tagged

Target Protein AA Sequence:

PRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK

Expression Region:

2-92aa

Subcellular Location:

Tissue Specificity:

Protein Length:

Full Length of Mature Protein

Pathway:

Mol. Weight:

14.3 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Others

Function:

In the E.coli 70S ribosome in the initiation state

Involvement in disease:

Relevance:

In the E.coli 70S ribosome in the initiation state it has been modeled to contact the 23S rRNA of the 50S subunit forming part of bridge B1a; this bridge is broken in the model with bound EF-G. The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states , contacting alternately S13 or S19. In the 3.5 angstroms resolved ribosome structures the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Universal ribosomal protein uS19 family

Reference:

Structures of the bacterial ribosome at 3.5 A resolution.Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.Science 310:827-834(2005)