OVA Peptide(257-264)

OVA Peptide(257-264);

OVA Peptide(257-264) 是 OVA 的 I 类 (Kb)-限制性肽表位,OVA 是由 I 类 MHC 分子 H-2Kb 呈递的来自卵清蛋白的八聚体肽。

OVA Peptide(257-264)amp;;

OVA Peptide(257-264) Chemical Structure

CAS No. : 138831-86-4

规格 是否有货
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OVA Peptide(257-264) 的其他形式现货产品:

OVA Peptide(257-264) TFA

生物活性

OVA Peptide(257-264) is a class I (Kb)-restricted peptide epitope of OVA, an octameric peptide from ovalbumin presented by the class I MHC molecule, H-2Kb.

体外研究
(In Vitro)

TAP1-I- and C57BL/6 macrophages may process Crl-OVA and full-length OVA in different cellular compartments and that the protein context of the OVA Peptide(257-264) epitope influences the extent of TAP-independent processing for MHC class I presentation. OVA Peptide(257-264) epitope is presented with a differential dependence on the TAP transporter depending on the protein context of the OVA epitope: OVA Peptide(257-264) contained within the MBPCrl-OVA or Crl-OVA bacterial fusion proteins is presented with little dependence on the TAP transporter, while OVA Peptide(257-264) contained within full-length ovalbumin is largely dependent on the TAP transporter, regardless of whether recombinant OVA is expressed in bacteria or the native protein is coupled to polystyrene beads[1].

MCE has not independently confirmed the accuracy of these methods. They are for reference only.

分子量

963.13

Formula

C45H74N10O13

CAS 号

138831-86-4

Sequence

Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu

Sequence Shortening

SIINFEKL

运输条件

Room temperature in continental US; may vary elsewhere.

储存方式

Please store the product under the recommended conditions in the Certificate of Analysis.

Solvent Solubility
In Vitro:;

H2O

Peptide Solubility and Storage Guidelines:

1.;;Calculate the length of the peptide.

2.;;Calculate the overall charge of the entire peptide according to the following table:

; Contents Assign value
Acidic amino acid Asp (D), Glu (E), and the C-terminal -COOH. -1
Basic amino acid Arg (R), Lys (K), His (H), and the N-terminal -NH2 +1
Neutral amino acid Gly (G), Ala (A), Leu (L), Ile (I), Val (V), Cys (C), Met (M), Thr (T), Ser (S), Phe (F), Tyr (Y), Trp (W), Pro (P), Asn (N), Gln (Q) 0

3.;;Recommended solution:

Overall charge of peptide Details
Negative (lt;0) 1.;;Try to dissolve the peptide in water first.
2.;;If water fails, add NH4OH (lt;50 μL).
3.;;If the peptide still does not dissolve, add DMSO (50-100 μL) to solubilize the peptide.
Positive (gt;0) 1.;;Try to dissolve the peptide in water first.
2.;;If water fails, try dissolving the peptide in a 10%-30% acetic acid solution.
3.;;If the peptide still does not dissolve, try dissolving the peptide in a small amount of DMSO.
Zero (=0) 1.;;Try to dissolve the peptide in organic solvent (acetonitrile, methanol, etc.) first.
2.;;For very hydrophobic peptides, try dissolving the peptide in a small amount of DMSO, and then dilute the solution with water to the desired concentration.
参考文献
  • [1]. Wick MJ, et al. Major histocompatibility complex class I presentation of ovalbumin peptide 257-264 from exogenous sources: protein context influences the degree of TAP-independent presentation. Eur J Immunol. 1996 Nov;26(11):2790-9.

Cell Assay

TAPl-/- or C57BL/6 macrophages are co-incubated with either bacteria or polystyrene beads containing the 257-264 epitope from ovalbumin [OVA Peptide(257-264)], which binds the mouse class I molecule Kb. The source of the OVA(257-264) epitope is either the Crl-OVA(257-264) (Crl-OVA) fusion protein, the maltose binding protein (MBP)-Crl-OVA fusion protein, native OVA or bacterial recombinant OVA (rOVA); Crl-OVA, MBP-Crl-OVA and rOVA are each expressed in bacteria, and Crl-OVA and MBP-Crl-OVA purified from bacterial lysates and native egg OVA are coated onto polystyrene beads[1].

MCE has not independently confirmed the accuracy of these methods. They are for reference only.

参考文献
  • [1]. Wick MJ, et al. Major histocompatibility complex class I presentation of ovalbumin peptide 257-264 from exogenous sources: protein context influences the degree of TAP-independent presentation. Eur J Immunol. 1996 Nov;26(11):2790-9.