Search: 107 results found for "sdf (cxcl12)"

Description:

Stem Cell Factor Mouse Recombinant

Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.

Product # :

CYT-275

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Description

Stem Cell Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18309 Dalton. The SCF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of Human TF-1 cell line is < 10 ng/ml, corresponding to a Specific Activity of 1x10⁵IU/mg.

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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Stem Cell Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MKEICGNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV IQLSLSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVLC MEENAPKNIK ESPKRPETRS FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.52 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Stem Cell Factor as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Succinate Dehydrogenase Complex Assembly Factor 2 Human Recombinant

Succinate dehydrogenase assembly factor 2 mitochondrial, SDH assembly factor 2, Succinate dehydrogenase subunit 5, mitochondrial, hSDH5, SDHAF2, C11orf79, PGL2, SDH5.

Product # :

PRO-593

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Description

SDHAF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (30-166 a.a) and having a molecular mass of 19kDa.SDHAF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SDHAF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Succinate Dehydrogenase Complex Assembly Factor 2 (SDHAF2) is a mitochondrial protein required for the flavination of a succinate dehydrogenase complex subunit essential for activity of the complex. DHAF2 is necessary for insertion of FAD cofactor into SDHA, the catalytic subunit of succinate dehydrogenase (SDH). SDH is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDHAF2 gene defects are the cause of hereditary paragangliomas type 2 (PGL2), otherwise known as familial non-chromaffin paragangliomas type 2.
Synonyms
Succinate dehydrogenase assembly factor 2 mitochondrial, SDH assembly factor 2, Succinate dehydrogenase subunit 5, mitochondrial, hSDH5, SDHAF2, C11orf79, PGL2, SDH5.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSFRRFYR GDSPTDSQKD MIEIPLPPWQ ERTDESIETK RARLLYESRK RGMLENCILL SLFAKEHLQH MTEKQLNLYD RLINEPSNDW DIYYWATEAK PAPEIFENEV MALLRDFAKN KNKEQRLRAP DLEYLFEKPR.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Colony Stimulating Factor Recombinant Rhesus Macaque

CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.

Product # :

CYT-1121

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Description

Granulocyte Colony Stimulating Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18.9kDa.GCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. 3 transcript variants encoding 3 different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that take part in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulocyte Colony Stimulating Rhesus Macaque should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Granulocyte Colony Stimulating Rhesus Macaque in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.
Background
What is the molecular weight/Mw of GCSF MONKEY Protein?
GCSF MONKEY Protein has a total Mw of 18.9kDa.

What is the source or expression system of GCSF MONKEY Protein?
Escherichia Coli.

What is the Purity of GCSF MONKEY Protein?
GCSF MONKEY Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GCSF MONKEY Protein?
The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.

What is the amino acid sequence of GCSF MONKEY Protein?
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.

What applications can GCSF MONKEY Protein be used in?
GCSF MONKEY Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GCSF MONKEY Protein?
The endotoxin level is minimal, GCSF MONKEY Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

IP-10 Rat Recombinant (CXCL10)

C-X-C motif chemokine 10, Gamma-IP10, IP-10, Protein Mob-1, Small-inducible cytokine B10, Cxcl10, Inp10, Mob1, Scyb10.

Product # :

CHM-264

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Description

IP-10 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8.6kDa.The IP-10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 10.0-50.0 ng/ml.

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Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types in response to IFN-?. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
Synonyms
C-X-C motif chemokine 10, Gamma-IP10, IP-10, Protein Mob-1, Small-inducible cytokine B10, Cxcl10, Inp10, Mob1, Scyb10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IP-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL10 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IP-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IPLARTVRCT CIDFHEQPLR PRAIGKLEII PASLSCPHVE IIATMKKNNE KRCLNPESEA IKSLLKAVSQ RRSKRAP.
Background
What is the molecular weight/Mw of CXCL10 RAT Protein?
CXCL10 RAT Protein has a total Mw of 8.6kDa.

What is the source or expression system of CXCL10 RAT Protein?
Escherichia Coli.

What is the Purity of CXCL10 RAT Protein?
CXCL10 RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL10 RAT Protein?
Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 10.0-50.0 ng/ml.

What is the amino acid sequence of CXCL10 RAT Protein?
IPLARTVRCT CIDFHEQPLR PRAIGKLEII PASLSCPHVE IIATMKKNNE KRCLNPESEA IKSLLKAVSQ RRSKRAP.

What applications can CXCL10 RAT Protein be used in?
CXCL10 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL10 RAT Protein?
The endotoxin level is minimal, CXCL10 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL10 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL10 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Lungkine (CXCL15) Mouse Recombinant

C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

Product # :

CHM-286

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Description

Recombinant Mouse Lungkine produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids and having a molecular mass of 16.4kDa.The CXCL15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Lungkine protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 0.02% Tween-20.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.

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Introduction
Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.
Synonyms
C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Lungkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL15 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Lungkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.
Background
What is the molecular weight/Mw of CXCL15 MOUSE Protein?
CXCL15 MOUSE Protein has a total Mw of 16.4kDa.

What is the source or expression system of CXCL15 MOUSE Protein?
Escherichia Coli.

What is the Purity of CXCL15 MOUSE Protein?
CXCL15 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL15 MOUSE Protein?
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.

What is the amino acid sequence of CXCL15 MOUSE Protein?
QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.

What applications can CXCL15 MOUSE Protein be used in?
CXCL15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL15 MOUSE Protein?
The endotoxin level is minimal, CXCL15 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL15 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL15 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Programmed Cell Death 12, Mouse Anti Human

Cell death regulator Aven, AVEN, PDCD12, Programmed Cell Death 12.

Product # :

ANT-457

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
PDCD12 (AVEN) represents a new class of cell death regulator. PDCD12 is a conserved intracellular membrane protein which blocks apoptosis impeded by Apaf-1 mediated caspase activation. BAD and Bcl-2 also interact with PDCD12 to prevent apoptosis. PDCD12 is expressed in a wide variety of normal tissues including the heart, skeletal muscle, kidney, liver, testis, and also in diseases such as cancer.
Synonyms
Cell death regulator Aven, AVEN, PDCD12, Programmed Cell Death 12.
Immunogen
Anti-human PDCD12 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PDCD12 amino acids 254-362 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
Clone
P3G4AT.
Applications
PDCD12 antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot is 1:1,000~1:2,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:1,000 and Immunohistochemistry is 1:50.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
PDCD12 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Macrophage-Colony Stimulating Factor Mouse Recombinant

CSF-1, Lanimostim, MCSF, M-CSF.

Product # :

CYT-439

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Description

Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5x10⁵ units/mg.

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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
CSF-1, Lanimostim, MCSF, M-CSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized M-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.
Background
Macrophage-Colony Stimulating Factor Mouse Recombinant: An In-Depth Analysis
Abstract:
Macrophage-Colony Stimulating Factor (M-CSF) is a crucial cytokine involved in the regulation of macrophage biology, including their differentiation, survival, and function. This research paper provides an in-depth analysis of M-CSF Mouse Recombinant, focusing on its structure, signaling pathways, and diverse functions in the context of human research. Additionally, the paper explores the therapeutic potential of M-CSF modulation in various diseases.
Introduction:
M-CSF plays a vital role in the development and maintenance of macrophages, key immune cells involved in innate immunity and tissue homeostasis. This paper aims to provide a comprehensive analysis of M-CSF Mouse Recombinant, highlighting its importance in human macrophage biology and its potential therapeutic applications.
Structure and Function of M-CSF:
M-CSF is a homodimeric protein that binds to its receptor, CSF-1R, leading to the activation of downstream signaling pathways. It regulates the proliferation, survival, and activation of macrophages, influencing immune responses and tissue remodeling processes.
Signaling Pathways:
Upon binding to CSF-1R, M-CSF triggers various intracellular signaling pathways, including the MAPK pathway, PI3K/Akt pathway, and JAK/STAT pathway. These pathways regulate gene expression and mediate cellular responses, impacting macrophage functions.
Role in Macrophage Development and Function:
M-CSF is essential for the differentiation and maturation of macrophages from hematopoietic progenitor cells. It promotes the survival, proliferation, and activation of macrophages, enhancing their phagocytic activity, cytokine production, and antigen presentation capabilities.
Therapeutic Potential:
Given its crucial role in macrophage biology, M-CSF modulation has emerged as a potential therapeutic strategy. M-CSF inhibitors and CSF-1R antagonists have shown promise in the treatment of inflammatory and autoimmune diseases, as well as certain cancers. Targeting M-CSF signaling can modulate immune responses and affect disease progression.
Clinical Applications and Future Directions:
The therapeutic potential of M-CSF modulation is being explored in various clinical settings. Clinical trials investigating M-CSF inhibitors as monotherapy or combination therapy are underway in diseases such as rheumatoid arthritis and cancer. Future research should focus on understanding the intricate mechanisms of M-CSF signaling, optimizing therapeutic strategies, and developing personalized treatment approaches.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

I-TAC Human Recombinant (CXCL11), His Tag

Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.

Product # :

CHM-232

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Shipped with Ice Packs

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Description

I-TAC (CXCL11) Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (22-94) and having a molecular mass of 10.6kDa.I-TAC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The I-TAC solution (1mg/ml) contains 10mM sodium citrate(pH 3.5), 20% glycerol and 2mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokine family that is also called Interferon-inducible T-cell alpha chemoattractant (I-TAC) and Interferon-gamma-inducible protein 9 (IP-9). It is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. This chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. CXCL11 is chemotactic for activated T cells. Its gene is located on human chromosome 4 along with many other members of the CXC chemokine family.
Synonyms
Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.
Background
What is the molecular weight/Mw of CXCL11 HUMAN, HIS Protein?
CXCL11 HUMAN, HIS Protein has a total Mw of 10.6kDa.

What is the source or expression system of CXCL11 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL11 HUMAN, HIS Protein?
CXCL11 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL11 HUMAN, HIS Protein?
The biological functionality of CXCL11 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.

What applications can CXCL11 HUMAN, HIS Protein be used in?
CXCL11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL11 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL11 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL11 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL11 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Thioredoxin Domain Containing 12 Human Recombinant

Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.

Product # :

PRO-1133

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Description

TXNDC12 Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (27-172) and having a molecular mass of 20.8 kDa.TXNDC12 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TXNDC12 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
TXNDC12 is a member of the thioredoxin super family. This Family members have a thioredoxin fold with a consensus active-site sequence (CxxC) and take part in redox regulation, protection against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors.
Synonyms
Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMHN GLGKGFGDHI HWRTLEDGKK EAAASGLPLM VIIHKSWCGA CKALKPKFAE STEISELSHN FVMVNLEDEE EPKDEDFSPD GGYIPRILFL DPSGKVHPEI INENGNPSYK YFYVSAEQVV QGMKEAQERL TGDAFRKKHL EDEL

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Macrophage Colony Stimulating Factor Mouse Recombinant, Sf9

M-Csf, Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, C87615, MCSF, op, Processedmacrophage colony-stimulating factor 1.

Product # :

CYT-1141

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Description

MCSF Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 164 amino acids (33-187 aa) and having a molecular mass of 19.1 kDa.MCSF is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The MCSF solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Determined by cell proliferation assay using M-NFS-60 mouse myelogenous leukemia lymphoblast cells. ED50 range for this effect is ≤ 4ng/ml.

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Introduction
Macrophage Colony Stimulating Factor (M CSF) or colony stimulating factor 1, is a cytokine, that promoted differentiation in hematopoietic stem cells to macrophages. Another role of M CSF is to bind to its receptor (colony stimulating factor 1 receptor) and to take part in placenta growth and development.
Synonyms
M-Csf, Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, C87615, MCSF, op, Processedmacrophage colony-stimulating factor 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPKEVSEHC SHMIGNGHLK VLQQLIDSQM ETSCQIAFEF VDQEQLDDPV CYLKKAFFLV
QDIIDETMRF KDNTPNANAT ERLQELSNNL NSCFTKDYEE QNKACVRTFH ETPLQLLEKI
KNFFNETKNL LEKDWNIFTK NCNNSFAKCS SRDVVTKPHH HHHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Stem Cell Factor Human Recombinant

Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.

Product # :

CYT-255

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Description

Stem Cell Factor Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18409 Dalton. The SCF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.

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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Stem Cell Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Gly-Ile-Cys.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.52 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Stem Cell Factor as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

GRO-Alpha Human Recombinant (CXCL1)

Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

Product # :

CHM-329

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Description

GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
Synonyms
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CXCL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
Background
What is the molecular weight/Mw of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein has a total Mw of 7.81kDa.

What is the source or expression system of CXCL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL1 HUMAN Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

What is the amino acid sequence of CXCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.

What applications can CXCL1 HUMAN Protein be used in?
CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL1 HUMAN Protein?
The endotoxin level is minimal, CXCL1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL1 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL1 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

BRAK Human Recombinant (CXCL14), His-Tag

C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.

Product # :

CHM-239

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Description

CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10.66 kDa. The Human BRAK contains a 10 a.a. fusion His tag at N-Terminus. The BRAK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CXCL14 filtered (0.4µm) and lyophilized from a concentrated (0.5mg/ml) solution containing 20mM Tris buffer & 20mM NaCl pH-7.5.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
Synonyms
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BRAK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BRAK should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CXCL14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS VSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
Background
What is the molecular weight/Mw of CXCL14 HUMAN, HIS Protein?
CXCL14 HUMAN, HIS Protein has a total Mw of 10.66kDa.

What is the source or expression system of CXCL14 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL14 HUMAN, HIS Protein?
CXCL14 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL14 HUMAN, HIS Protein?
The biological functionality of CXCL14 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL14 HUMAN, HIS Protein?
MKHHHHHHAS SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS VSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.

What applications can CXCL14 HUMAN, HIS Protein be used in?
CXCL14 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL14 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL14 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL14 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL14 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cerebral Neurotrophic Factor Human Recombinant

Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.

Product # :

CYT-167

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Description

CDNF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L
Background
Cerebral Neurotrophic Factor Human Recombinant: A Leap Forward in Neurobiology
The field of neurobiology is replete with wonder, particularly due to the influential role of neurotrophic factors. These essential proteins, responsible for the survival and growth of neurons, have become a focal point in modern research. Among these, the Cerebral Neurotrophic Factor (CNF) stands out, offering novel insights and potential breakthroughs in our understanding of neurological health.
Enter the world of bioengineering, a scientific arena where we have successfully replicated CNF, leading to the birth of Cerebral Neurotrophic Factor Human Recombinant (CNF-HR). This is a massive step towards conquering neurodegenerative disorders such as Alzheimer's and Parkinson's diseases, conditions that have perplexed scientists and clinicians for decades.
The extraordinary capacity of CNF-HR lies in its dual functionality - it acts as a defender and a promoter. It defends neurons from harmful degenerative processes while promoting their growth and development. Picture a devoted gardener who tirelessly protects his garden from pests and nurtures the growth of each plant. In this context, the brain is the vibrant garden, and the neurons, the delicate plants we must care for.
Although this scientific breakthrough sparks enthusiasm, it's crucial to remember the challenges that lie ahead. The path to determining the most effective method of delivering CNF-HR to the brain, identifying the optimal dosage, and monitoring potential side effects is a winding one. Nevertheless, with continuous research and relentless scientific curiosity, we are optimistic about overcoming these challenges.
In conclusion, the development of CNF-HR is a significant milestone in the fascinating journey of neurobiology. Its potential to change the trajectory of treating neurodegenerative diseases and enhancing our understanding of neuronal function is tremendous. While the journey is strewn with complexities, the potential rewards we stand to reap promise a future where neurodegenerative diseases could be effectively managed or even cured.
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.5kDa.

What is the source or expression system of CDNF Protein?
Escherichia Coli.

What is the Purity of CDNF Protein?
CDNF Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of CDNF Protein?
The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

What is the amino acid sequence of CDNF Protein?
QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L

What applications can CDNF Protein be used in?
CDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CDNF Protein?
The endotoxin level is minimal, CDNF Protein was purified using conventional chromatography techniques

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

Product # :

CYT-1095

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Description

Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant produced in E. coli is a non-glycosylated monomer chain containing 128 amino acids and having a molecular mass of 14.5kDa. GMCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as determined by TF-1 cell proliferation is 4.52ng/ml corresponding to a specific activity which is 2.2 x 10^5 units/mg.

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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of GMCSF is found extracellularly as a homodimer. GMCSF has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK.
Background
What is the molecular weight/Mw of GM-CSF PORCINE Protein?
GM-CSF PORCINE Protein has a total Mw of 14.5kDa.

What is the source or expression system of GM-CSF PORCINE Protein?
Escherichia Coli.

What is the Purity of GM-CSF PORCINE Protein?
GM-CSF PORCINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF PORCINE Protein?
The ED50, as determined by TF-1 cell proliferation is 4.52ng/ml corresponding to a specific activity which is 2.2 x 10^5 units/mg.

What is the amino acid sequence of GM-CSF PORCINE Protein?
MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK.

What applications can GM-CSF PORCINE Protein be used in?
GM-CSF PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF PORCINE Protein?
The endotoxin level is minimal, GM-CSF PORCINE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

IP-10 (CXCL10) Guinea Pig Recombinant

CXCL10, CRG-2.

Product # :

CHM-046

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Description

IP10 Guinea Pig Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a total molecular mass of 8.7kDa.The IP10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 10 mM Sodium Phosphate, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
Synonyms
CXCL10, CRG-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IP10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IP10 Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IP10 in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IPHSRTIRCT CIETSTQPVN PKSFKKLEII PASQSCPRVE IIATMKMNGE KRCLDPESKV IKNLLKAVRK ERSKRS
Background
What is the molecular weight/Mw of CXCL10 GUINEA PIG Protein?
CXCL10 GUINEA PIG Protein has a total Mw of 8.7kDa.

What is the source or expression system of CXCL10 GUINEA PIG Protein?
Escherichia Coli.

What is the Purity of CXCL10 GUINEA PIG Protein?
CXCL10 GUINEA PIG Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL10 GUINEA PIG Protein?
The biological functionality of CXCL10 GUINEA PIG Protein will be determined in the future.

What is the amino acid sequence of CXCL10 GUINEA PIG Protein?
IPHSRTIRCT CIETSTQPVN PKSFKKLEII PASQSCPRVE IIATMKMNGE KRCLDPESKV IKNLLKAVRK ERSKRS

What applications can CXCL10 GUINEA PIG Protein be used in?
CXCL10 GUINEA PIG Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL10 GUINEA PIG Protein?
The endotoxin level is minimal, CXCL10 GUINEA PIG Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL10 GUINEA PIG that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL10 GUINEA PIG?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

GM-CSF Receptor Alpha Sf9 Human Recombinant

Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.

Product # :

CYT-1044

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Description

CSF2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (20-320a.a.) and having a molecular mass of 35.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CSF2RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CSF2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

More Info

Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
Synonyms
Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPLIPEKSD LRTVAPASSL NVRFDSRTMN LSWDCQENTT FSKCFLTDKK NRVVEPRLSN NECSCTFREI CLHEGVTFEV HVNTSQRGFQ QKLLYPNSGR EGTAAQNFSC FIYNADLMNC TWARGPTAPR DVQYFLYIRN SKRRREIRCP YYIQDSGTHV GCHLDNLSGL TSRNYFLVNG TSREIGIQFF DSLLDTKKIE RFNPPSNVTV RCNTTHCLVR WKQPRTYQKL SYLDFQYQLD VHRKNTQPGT ENLLINVSGD LENRYNFPSS EPRAKHSVKI RAADVRILNW SSWSEAIEFG SDDGHHHHHH
Background
GM-CSF Receptor Alpha Human Recombinant: A Glimpse into Its Potential and Implications
Abstract:
Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) receptor alpha, a pivotal component in the GM-CSF signaling pathway, has been the focal point of numerous studies pertaining to hematopoiesis and immune responses. This paper provides an overview of the GM-CSF receptor alpha human recombinant, exploring its characteristics, production techniques, and potential therapeutic applications.
Introduction
GM-CSF, a cytokine responsible for the differentiation and proliferation of white blood cells, functions by binding to its receptor, GM-CSF receptor. The alpha subunit (GM-CSFRα) of this receptor plays a crucial role in ligand binding and is essential for initiating cellular responses. Modern biotechnological advancements have led to the successful production of its human recombinant form, offering new avenues in medical research.
Recombinant GM-CSFRα:
Production and Features Recombinant GM-CSFRα is synthesized using cutting-edge recombinant DNA technologies, predominantly in bacterial or mammalian expression systems. This human recombinant form retains its ability to bind to GM-CSF, maintaining its biological functionality and providing myriad research opportunities.
Therapeutic and Clinical Prospects
1. Autoimmune Diseases: GM-CSF is often overexpressed in various autoimmune disorders. By utilizing recombinant GM-CSFRα as a potential decoy receptor, it's feasible to mitigate the effects of excessive GM-CSF, offering a new therapeutic strategy.
2. Hematopoietic Disorders: Given its integral role in white blood cell development, recombinant GM-CSFRα might hold promise in treatments or as a diagnostic tool for certain hematological conditions.
3. Research Paradigm: Beyond therapeutic applications, the recombinant GM-CSFRα can serve as an invaluable research tool to elucidate the nuances of GM-CSF signaling, aiding in the understanding of immune response mechanisms.
Conclusion:
GM-CSF receptor alpha human recombinant stands at the forefront of exciting research and therapeutic potential. While its full capabilities are yet to be realized, current insights underscore its significance in the realms of immunology and medicine.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 35.9kDa.

What is the source or expression system of CD116 Protein?
Sf9, Baculovirus cells.
What is the Purity of CD116 Protein?
CD116 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CD116 Protein?
Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 310 amino acids.

What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 Protein was purified using conventional chromatography techniques

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Macrophage Colony Stimulating Factor Human Recombinant, Baculovirus

CSF-1, Lanimostim, MCSF, MGC31930, M-CSF, Macrophage colony-stimulating factor 1, CSF1.

Product # :

CYT-637

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Description

Macrophage Colony Stimulating Factor Human Recombinant produced in Baculovirus is a disulfide linked homodimer, glycosylated, polypeptide chain containing 2 x 149 amino acids and having a total molecular mass of 42 kDa.MCSF is purified by proprietary chromatographic techniques.

Source

Baculovirus infected Silkworm.

Formulation

The lyophilized protein (1mg/ml) was lyophilized with 20mM phosphate buffer, 1% HSA and 3% manntiol.

Purity

Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells was found < 3ng/ml, corresponding to a specific activity of less than 333,333.33units/mg.

More Info

Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF, Macrophage colony-stimulating factor 1, CSF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EEVSEYCSHM IGSGHLQSLQ RLIDSQMETS CQITFEFVDQ EQLKDPVCYL KKAFLLVQDI MEDTMRFRDN TPNAIAIVQL QELSLRLKSC FTKDYEEHDK ACVRTFYETP LQLLEKVKNV FNETKNLLDK DWNIFSKNCN NSFAECSSQ.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

IP-10 Rhesus macaque Recombinant (CXCL10)

C-X-C motif chemokine 10, 10 kDa, Gamma-IP10, IP-10, Small-inducible cytokine B10, CXCL10, SCYB10.

Product # :

CHM-010

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Description

IP-10 Rhesus macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8.7kDa. The IP-10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human peripheral blood T-Lymphocytes using a concentration range of 10.0-100.0 ng/ml.

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Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family that is also known as 10 kDa IP-10. CXCL10 is secreted by several cell types in response to IFN-?. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
Synonyms
C-X-C motif chemokine 10, 10 kDa, Gamma-IP10, IP-10, Small-inducible cytokine B10, CXCL10, SCYB10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IP-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL10 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IP-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IPLSRTVRCT CISISNQPVN PRSLEKLEII PPSQFCPHVE IIATMKKKGE KRCLNPESKA IKNLLKAVSK ERSKRSP.
Background
What is the molecular weight/Mw of CXCL10 MACAQUE Protein?
CXCL10 MACAQUE Protein has a total Mw of 8.7kDa.

What is the source or expression system of CXCL10 MACAQUE Protein?
Escherichia Coli.

What is the Purity of CXCL10 MACAQUE Protein?
CXCL10 MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL10 MACAQUE Protein?
Determined by its ability to chemoattract human peripheral blood T-Lymphocytes using a concentration range of 10.0-100.0 ng/ml.

What is the amino acid sequence of CXCL10 MACAQUE Protein?
IPLSRTVRCT CISISNQPVN PRSLEKLEII PPSQFCPHVE IIATMKKKGE KRCLNPESKA IKNLLKAVSK ERSKRSP.

What applications can CXCL10 MACAQUE Protein be used in?
CXCL10 MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL10 MACAQUE Protein?
The endotoxin level is minimal, CXCL10 MACAQUE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL10 MACAQUE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL10 MACAQUE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Sf9

CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

Product # :

CYT-416

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Shipped at Room temp

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Description

GM-CSF Human Recombinant produced in insect cells is a single, glycosylated, polypeptide chain containing 127 amino acids (18-144) and having a molecular mass of 14.6kDa. GM-CSF is fused to a C-terminal His -tag (6x His) and purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

The protein was lyophilized with PBS.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

More Info

Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
Background
Recombinant Granulocyte-Macrophage Colony-Stimulating Factor (GMCSF) is a protein that plays a crucial role in the production and differentiation of white blood cells, including granulocytes and macrophages. It is a potent stimulator of hematopoietic stem cells, which are responsible for the production of all blood cells in the body. Recombinant GMCSF is a synthetic version of the protein that is produced using recombinant DNA technology.
Recombinant GMCSF has been extensively studied for its potential therapeutic applications in a variety of medical conditions, including cancer, autoimmune diseases, and infectious diseases. In cancer, GMCSF is used as an immunostimulatory agent to enhance the immune response against cancer cells. By stimulating the production and differentiation of white blood cells, GM-CSF can increase the number of immune cells that can recognize and attack cancer cells. This approach has been successfully used in the treatment of several types of cancer, including melanoma and leukemia.
In autoimmune diseases, recombinant GMCSF has been investigated as a potential treatment for conditions such as rheumatoid arthritis and multiple sclerosis. These diseases are characterized by an overactive immune response that attacks healthy tissues in the body. By modulating the immune response, GMCSF may be able to reduce inflammation and prevent further damage to affected tissues.
In infectious diseases, recombinant GMCSF has been studied as a potential treatment for conditions such as sepsis and HIV/AIDS. In sepsis, a severe bacterial infection, GMCSF may be able to stimulate the production of white blood cells and improve the immune response against the infection. In HIV/AIDS, GMCSF may be able to enhance the immune response against the virus and reduce the risk of opportunistic infections.
Recombinant GMCSF is typically administered by injection, either directly into the affected tissue or into the bloodstream. It is generally well-tolerated, although some patients may experience side effects such as fever, fatigue, and muscle pain.
In conclusion, recombinant GMCSF is a promising therapeutic agent with potential applications in a variety of medical conditions. Its ability to stimulate the production and differentiation of white blood cells makes it a valuable tool in the treatment of cancer, autoimmune diseases, and infectious diseases. Ongoing research is likely to uncover new uses for this protein and further refine its therapeutic potential.
What is the molecular weight/Mw of GM- CSF HUMAN, SF9 Protein?
GM- CSF HUMAN, SF9 Protein has a total Mw of 14.6kDa.

What is the source or expression system of GM- CSF HUMAN, SF9 Protein?
Insect Cells.
What is the Purity of GM- CSF HUMAN, SF9 Protein?
GM- CSF HUMAN, SF9 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GM- CSF HUMAN, SF9 Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of GM- CSF HUMAN, SF9 Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

What applications can GM- CSF HUMAN, SF9 Protein be used in?
GM- CSF HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM- CSF HUMAN, SF9 Protein?
The endotoxin level is minimal, GM- CSF HUMAN, SF9 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Dnak Substrate Binding Domain C-terminal E.Coli Recombinant

HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

Product # :

HSP-009

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Description

Recombinant Dnak Substrate Binding Domain C-terminal produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids and having a molecular mass of 27.7 kDa.

Source

Escherichia Coli.

Formulation

The DnaK protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.The protein coding region of the substrate binding domain of DnaK (amino acids 385-638) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.
Synonyms
HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQGERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HSTRKQVEEA GDKLPADDKTAIESALTALE TALKGEDKAA IEAKMQELAQ VSQKLMEIAQ QQHAQQQTAG ADASANNAKD DDVVDAEFEE VKDKK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

TNF Ligand Receptor Superfamily Member 12A Human Recombinant, Sf9

Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.

Product # :

CYT-1021

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Description

TNFRSF12A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (28-80a.a.) and having a molecular mass of 32.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). TNFRSF12A is expressed with a 239 amino acids hIgG- His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF12A protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
The gene for TNFRSF12A was initially recognized as a fibroblast growth factor inducible immediate early response gene Fn14 in mouse NIH 3T3 fibroblasts. Human TNFRSF12A cDNA encodes a 129 amino acid residue type I transmembrane protein with a 27 aa signal peptide, a 53 aa extracellular domain, a 21 aa transmembrane domain and a 28 aa cytoplasmic domain. Human and mouse TNFRSF12A hold 82% aa sequence identity. TNFRSF12 is the tiniest member of the TNF receptor superfamily and has only one cysteine rich region in its extracellular domain. The TNFRSF12A cytoplasmic domain holds one TRAF binding motif which binds TRAFs 1, 2, and 3. TNFRSF12A binds its ligand TWEAK/TNFSF12A with high affinity to initiate a signal transduction cascade which subject to the cell type, causes different cellular responses such as cell death, cell proliferation, and angiogenesis.
Synonyms
Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWPLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Sulfatase Modifying Factor 1 Human Recombinant, Sf9

SUMF1, AAPA3037, FGE, UNQ3037, Formylglycine-generating enzyme, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 1.

Product # :

PRO-2619

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Quantity :

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Description

SUMF1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 347 amino acids (34-374.a.) and having a molecular mass of 38.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). SUMF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

SUMF1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
SUMF1 is a part of the SUMF protein family. SUMF1 catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue called C-alpha-formylglycine. Mutations in this gene will cause multiple sulfatase deficiency meaning a lysosomal storage disorder.
Synonyms
SUMF1, AAPA3037, FGE, UNQ3037, Formylglycine-generating enzyme, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
SQEAGTGAGA GSLAGSCGCG TPQRPGAHGS SAAAHRYSRE ANAPGPVPGE RQLAHSKMVP IPAGVFTMGT DDPQIKQDGE APARRVTIDA FYMDAYEVSN TEFEKFVNST GYLTEAEKFG DSFVFEGMLS EQVKTNIQQA VAAAPWWLPV KGANWRHPEG PDSTILHRPD HPVLHVSWND AVAYCTWAGK RLPTEAEWEY SCRGGLHNRL FPWGNKLQPK GQHYANIWQG EFPVTNTGED GFQGTAPVDA FPPNGYGLYN IVGNAWEWTS DWWTVHHSVE ETLNPKGPPS GKDRVKKGGS YMCHRSYCYR YRCAARSQNT PDSSASNLGF RCAADRLPTM DHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Rhesus Macaque Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

Product # :

CYT-720

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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Description

Granulocyte Macrophage Colony Stimulating Factor Monkey Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.4 kDa.GM-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GM-CSF was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH 7.4.

Purity

Greater than 98.0% as determined by SDS-PAGE and RP-HPLC.

Biological Activity

The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 IU/mg.

More Info

Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13. GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APARSPSPGT QPWEHVNAIQ EARRLLNLSR DTAAEMNKTV EVVSEMFDLQ EPSCLQTRLE LYKQGLQGSL TKLKGPLTMM ASHYKQHCPP TPETSCATQI ITFQSFKENL KDFLLVIPFD CWEPVQE.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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