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  5. CD27 Ligand/CD70
  6. CD70 Protein, Human (HEK293, His-Flag)

As a ligand of CD27, CD70 protein is an indispensable part of T cell immune coordination and is of particular importance in antiviral responses. The CD70-CD27 pathway emerged as a key player that contributes to the generation and maintenance of T cell-mediated immune responses. CD70 Protein, Human (HEK293, His-Flag) is the recombinant human-derived CD70 protein, expressed by HEK293, with N-His and N-Flag labeled tag.

For research use only. We do not sell to patients.

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Description

As a ligand of CD27, CD70 protein is an indispensable part of T cell immune coordination and is of particular importance in antiviral responses. The CD70-CD27 pathway emerged as a key player that contributes to the generation and maintenance of T cell-mediated immune responses. CD70 Protein, Human (HEK293, His-Flag) is the recombinant human-derived CD70 protein, expressed by HEK293, with N-His and N-Flag labeled tag.

Background

CD70, a cytokine functioning as the ligand for CD27, is integral to the CD70-CD27 pathway, which holds a crucial role in the development and sustenance of T cell immunity, especially in antiviral responses. Upon binding to CD27, CD70 induces the proliferation of costimulated T-cells and amplifies the generation of cytolytic T-cells, contributing to an effective immune response. Structurally, CD70 forms homotrimers, reflecting its molecular organization. The CD70-CD27 interaction underscores its significance in orchestrating T cell-mediated immune responses, providing valuable insights into the regulation of immune functions.

Species

Human

Source

HEK293

Tag

N-His;N-Flag

Accession

P32970-1 (S52-P193)

Gene ID

970

Molecular Construction
N-term
His
Flag
CD70 (S52-P193)
Accession # P32970-1
C-term
Protein Length

Partial

Synonyms
CD70 antigen; CD70; CD27 ligand; CD27LG; TNFSF7; CD27L
Predicted Molecular Mass
49.3 kDa
Molecular Weight

Approximately 50-60 kDa,based on SDS-PAGE under non-reduced conditions,due to the glycosylation.

Glycosylation
Yes
Structure/Form
Monomer
Purity

Greater than 95% as determined by reducing SDS-PAGE.

Appearance

Lyophilized powder.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Storage & Stability

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Lyophilized powder.

Documentation

CD70 Protein, Human (HEK293, His-Flag) Related Classifications

Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

  • Reconstitution Calculator

  • Dilution Calculator

  • Specific Activity Calculator

The reconstitution calculator equation

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration
= ÷

The dilution calculator equation

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
× = ×
C1   V1   C2   V2

The specific activity calculator equation

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)
Unit/mg = 106 ÷ ng/mL

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Product Name:
CD70 Protein, Human (HEK293, His-Flag)
Cat. No.:
HY-P704364
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