Search: 1000 results found for "glycophorin"

Description:

Macrophage-Derived Chemokine Human Recombinant (CCL22), His Tag

C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

Product # :

CHM-367

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SDS-PAGE

Description

MDC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 90 amino acids (25-93 a.a.) and having a molecular mass of 10.3 kDa. The MDC is fused to 21 amino acid His-Tag at N-terminus purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MDC protein contains phosphate-buffered Saline (PBS) pH7.4 and 10% glycerol.

Purity

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

SDS-PAGE

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Introduction
MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.
Synonyms
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.
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
MGSSHHHHHH SSGLVPRGSH MGPYGANMED SVCCRDYVRY RLPLRVVKHF YWTSDSCPRP GVVLLTFRDK EICADPRVPW VKMILNKLSQ.
Background
What is the molecular weight/Mw of CCL22 HUMAN, HIS Protein?
CCL22 HUMAN, HIS Protein has a total Mw of 10.3kDa.

What is the source or expression system of CCL22 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL22 HUMAN, HIS Protein?
CCL22 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL22 HUMAN, HIS Protein?
The biological functionality of CCL22 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL22 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGPYGANMED SVCCRDYVRY RLPLRVVKHF YWTSDSCPRP GVVLLTFRDK EICADPRVPW VKMILNKLSQ

What applications can CCL22 HUMAN, HIS Protein be used in?
CCL22 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL22 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL22 HUMAN, HIS 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:

Connective Tissue Growth Factor Human Recombinant , HEK

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.

Product # :

CYT-687

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Description

The CTGF Human Recombinant produced in HEK293 cells, is 36kDa protein containing a total of 329 amino acid residues (aa 27-349) including a C-terminal 6×His tag.

Source

HEK293 cells.

Formulation

CTGF filtered (0.2µm) solution in 0.1M Citrate buffer pH 4.7 and 20% (w/v) glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.
Physical Appearance
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
QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.
Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 36kDa.

What is the source or expression system of CTGF Protein?
HEK293 cells.

What is the Purity of CTGF Protein?
CTGF Protein is >90% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of CTGF Protein?
QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.

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

What is the endotoxin level for CTGF Protein?
The endotoxin level is minimal, CTGF 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:

Matrix Metalloproteinase-7 Human Recombinant

Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.

Product # :

ENZ-867

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Description

MMP-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (95-267 a.a) and having a molecular mass of 19.2kDa.MMP7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MMP7 protein solution (1mg/ml) containing 20mM Tris 8.0 and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
Synonyms
Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.
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
MYSLFPNSPK WTSKVVTYRI VSYTRDLPHI TVDRLVSKAL NMWGKEIPLH FRKVVWGTAD IMIGFARGAH GDSYPFDGPG NTLAHAFAPG TGLGGDAHFD EDERWTDGSS LGINFLYAAT HELGHSLGMG HSSDPNAVMY PTYGNGDPQN FKLSQDDIKG IQKLYGKRSN SRKK.

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:

Coronavirus NL63 Recombinant

Product # :

SARS-003

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Description

Recombinant Coronavirus NL63 c-terminal nucleoprotein produced in E. coli contains 221-340 amino acids and fused to a 6 a.a. His tag a c-terminal having a total of 130 a.a..

Source

Escherichia Coli.

Formulation

Coronavirus NL63 protein solution is supplied in PBS and 25mM K2CO3.

Purity

Protein is >95% pure as determined by 10% SDS-PAGE (coomassie staining).

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Introduction
Human coronavirus NL63 also known as HCoV-NL63 is a type of coronavirus that was identified in 2004. Among the associated diseases are mild to moderate upper respiratory tract infections, bronchiolitis, severe lower respiratory tract infection and croup. Coronavirus NL63 appears mainly in young children, the elderly and immunocompromised patients with acute respiratory illness. Coronavirus NL63 has a seasonal association in temperate climates. Coronavirus NL63 is not an emerging virus, but rather one that continually circulates the human population. Transmission of HCoV-NL63 is likely through droplet expulsion from the respiratory tract, which may be cottages when close personal contact occurs. Coronavirus NL63 is able to endure for up to7 days in respiratory secretions and remains infective at room temperature. Once the virus has entered the host it binds to cellular receptors using spike proteins, similar to those found in HIV-1. Coronavirus NL63 is able to use Angiotensin-converting enzyme 2 (ACE2) as an entry receptor to target cells. Since coronavirus NL63 is a positive single-stranded RNA virus, the processes of replication via transcription and translation can be carried out in the cytoplasm of the infected cell.
Physical Appearance
Sterile Filtered clear 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
GSSQPRADKPSQLKKPRWKRVPTREENVIQCFGPRDFNHNMGDSDLVQNGVDA
KGFPQLAELIPNQAALFFDSEVSTDEVGDNVQITYTYKMLVAKDNKNLPKFIEQISAF
TKPSSIKEMQSLEHHHHHH

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:

Capping Protein Gelsolin-Like, Mouse Anti Human

AFCP, CAPG, Macrophage-capping protein, Actin regulatory protein CAP-G, MCP.

Product # :

ANT-643

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
CAPG is part of the gelsolin/villin family of actin-regulatory proteins. CAPG reversibly blocks the barbed ends of F-actin filaments in a Ca2+ and phosphoinositide-regulated method, though it does not separate preformed actin filaments. By capping the barbed ends of actin filaments, CAPG contributes to the control of actin-based motility in non-muscle cells. CAPG is involved in macrophage function. CAPG is involved in regulating cytoplasmic and/or nuclear structures via possible interactions with actin. CAPG binds DNA. CAPG lacks a nuclear export sequence present in structurally related proteins. CAPG is a tumor suppressor protein that plays a role in the tumorigenic progression of certain cancers. Dysregulated expression of CAPG was found in premalignant and malignant oral carcinogenesis.
Synonyms
AFCP, CAPG, Macrophage-capping protein, Actin regulatory protein CAP-G, MCP.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human CAPG mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CAPG amino acids 1-348 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PAT1D10AT.
Applications
CAPG antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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
CAPG antibody was purified from mouse ascitic fluids by protein-A 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:

Adiponectin Human Recombinant, Sf9

Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

Product # :

CYT-1002

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sds-page

Description

Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

Acrp30 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

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Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.
Synonyms
Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.
Physical Appearance
Sterile Filtered clear 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
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.9kDa.

What is the source or expression system of ADIPONECTIN Protein?
Sf9, Baculovirus cells.

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

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

What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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:

Galectin-1 Human Recombinant

Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.

Product # :

CYT-544

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Shipped at Room temp

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Description

LGALS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids and having a molecular mass of 14.7kDa.The LGALS1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Galectin-1 protein was lyophilized from a concentrated (1mg/ml) containing 10mM sodium phosphate, pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity of Human Galectin-1 which is determined by the ability to induce chemotaxis of human THP-1 cells is detectable starting at 100ng/ml, corresponding to a specific activity of 1.0x10⁴ units/mg.

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Introduction
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. Galectin-1 is an autocrine negative growth factor that regulates cell proliferation. Galectin-1 regulates cell apoptosis and cell differentiation. Galectin-1 binds CD45, CD3 and CD4 & inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of lyn kinase. Galectin-1 and its ligands are one of the master regulators of immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host–pathogen interactions. Galectin-1 expression or overexpression in tumors and/or the tissue surrounding them must be considered as a sign of the malignant tumor progression that is often related to the long-range dissemination of tumoral cells (metastasis), to their dissemination into the surrounding normal tissue, and to tumor immune-escape. Galectin-1 in its oxidized form plays a number of important roles in the regeneration of the central nervous system after injury. The targeted overexpression (or delivery) of Galectin-1 should be considered as a method of choice for the treatment of some kinds of inflammation-related diseases, neurodegenerative pathologies and muscular dystrophies. In contrast, the targeted inhibition of Galectin-1 expression is what should be developed for therapeutic applications against cancer progression. Galectin-1 is thus a promising molecular target for the development of new and original therapeutic tools. There is 88% homology between the human and mouse galectin-1.
Synonyms
Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Galectin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-1 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 LGALS1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD.
Background
What is the molecular weight/Mw of LGALS1 HUMAN Protein?
LGALS1 HUMAN Protein has a total Mw of 14.7kDa.

What is the source or expression system of LGALS1 HUMAN Protein?
Escherichia Coli.

What is the Purity of LGALS1 HUMAN Protein?
LGALS1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS1 HUMAN Protein?
The activity of Human Galectin-1 which is determined by the ability to induce chemotaxis of human THP-1 cells is detectable starting at 100ng/ml, corresponding to a specific activity of 1.0x104 units/mg.

What is the amino acid sequence of LGALS1 HUMAN Protein?
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD.

What applications can LGALS1 HUMAN Protein be used in?
LGALS1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS1 HUMAN Protein?
The endotoxin level is minimal, LGALS1 HUMAN Protein was purified using conventional chromatography techniques.
Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.59 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).

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:

Proheparin-Binding EGF-like Growth Factor Rat Recombinant

Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.

Product # :

CYT-170

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Shipped at Room temp

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Description

HB-EGF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa.The HB-EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was filtered (0.2µm) and lyophilized from a concentrated solution containing PBS, 300mM NaCl, pH 7.4 and 5% trehalose.

Purity

Greater than 95.0% 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 balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×10⁶ units/mg.

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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind heparin and heparin sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
Synonyms
Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF 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 Rat HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.
Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.7kDa.

What is the source or expression system of HB-EGF Protein?
Escherichia Coli.

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

What is the Biological Activity of HB-EGF Protein?
The ED50 as determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.

What is the amino acid sequence of HB-EGF Protein?
DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.

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

What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-EGF 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:

Lymphocyte Antigen 9 Human Recombinant

Lymphocyte Antigen 9, Signaling Lymphocytic Activation Molecule 3, Cell Surface Molecule Ly-9, SLAM Family Member 3, SLAMF3, CD229 Antigen, CD229, Hly9, MLY9, LY9.

Product # :

PRO-2338

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Description

LY9 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 416 amino acids (48-454 aa) and having a molecular mass of 45.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).LY9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

LY9 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Lymphocyte Antigen 9, also known as LY9 is a member of the SLAM family of immunomodulatory receptors, LY9 interacts with the adaptor molecule SAP . LY9 plays a part in adhesion reactions between T lymphocytes and accessory cells via homophilic interaction. LY9 promotes T-cell differentiation into a helper T-cell Th17 phenotype which leads to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Furthermore it also promotes recruitment of RORC to the IL-17 promoter. LY9 is implicated in the maintenance of peripheral cell tolerance through serving as a negative regulator of the immune response. LY9 disables autoantibody responses as well as inhibits IFN-gamma secretion by CD4(+) T-cells. Moreover, LY9 negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells. Systemic Lupus Erythematosus is one of the diseases which are associated with LY9.
Synonyms
Lymphocyte Antigen 9, Signaling Lymphocytic Activation Molecule 3, Cell Surface Molecule Ly-9, SLAM Family Member 3, SLAMF3, CD229 Antigen, CD229, Hly9, MLY9, LY9.
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
ADLKDSAPTV VSGILGGSVT LPLNISVDTE IENVIWIGPK NALAFARPKE NVTIMVKSYL GRLDITKWSY SLCISNLTLN DAGSYKAQIN QRNFEVTTEE EFTLFVYEQL QEPQVTMKSV KVSENFSCNI TLMCSVKGAE KSVLYSWTPR EPHASESNGG SILTVSRTPC DPDLPYICTA QNPVSQRSSL PVHVGQFCTD PGASRGGTTG ETVVGVLGEP VTLPLALPAC RDTEKVVWLF NTSIISKERE EAATADPLIK SRDPYKNRVW VSSQDCSLKI SQLKIEDAGP YHAYVCSEAS SVTSMTHVTL LIYRRLRKPK ITWSLRHSED GICRISLTCS VEDGGNTVMY TWTPLQKEAV VSQGESHLNV SWRSSENHPN LTCTASNPVS RSSHQFLSEN ICSGPERNTK HHHHHH

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:

Erythropoietin Rat Recombinant

Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.

Product # :

CYT-1187

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sds-page

Description

EPO Rat Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-192 a.a) containing 175 amino acids and having a molecular mass of 19.6 kDa. EPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

EPO protein (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

sds-page

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Introduction
Erythropoietin or EPO is a hormone (glycoprotein), part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.
Synonyms
Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.
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
DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.
Background
What is the molecular weight/Mw of EPO Protein?
EPO Protein has a total Mw of 19.6kDa.

What is the source or expression system of EPO Protein?
HEK293 cells.

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

What is the Biological Activity of EPO Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

What is the amino acid sequence of EPO Protein?
DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.

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

What is the endotoxin level for EPO Protein?
The endotoxin level is minimal, EPO 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:

Pro-Nerve Growth Factor Human Recombinant

Human Pro-NGF, ProNGF, NGFB.

Product # :

CYT-426

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Pro-NGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 25 kDa.ProNGF Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ProNGF was lyophilized from a 0.2 μM filtered solution of 20m Tris-HCL, 0.5M NaCl, 5% Trehalose, 5% Mannitol. 0.01% Tween-80 and 1mM EDTA pH-8.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Human Pro-NGF, ProNGF, NGFB.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ProNGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProNGF 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 ProNGF in distilled water to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
VCVLSRKAVRRA.
Background
Pro-Nerve Growth Factor Human Recombinant: Unveiling its Potential in Neuroregulation and Disease Pathogenesis
Abstract:
Pro-Nerve Growth Factor (Pro-NGF) human recombinant is a crucial precursor protein involved in neuronal development, survival, and degenerative processes. This research paper aims to provide a comprehensive analysis of Pro-NGF, including its characteristics, processing mechanisms, and implications in neuroregulation and disease pathogenesis. Additionally, innovative methodologies for the production and manipulation of Pro-NGF human recombinant are proposed, highlighting its potential as a therapeutic target for neurological disorders and neurodegenerative diseases.
Introduction:
Neuroregulation and maintenance of neuronal health are intricate processes governed by a network of signaling molecules. Pro-NGF, the precursor form of Nerve Growth Factor (NGF), acts as a key player in neuronal development, synaptic plasticity, and cell survival. This paper delves into the distinctive features of Pro-NGF and presents novel approaches for the production and manipulation of Pro-NGF human recombinant, aiming to unravel its role in neuroregulation and disease pathogenesis.
Characteristics and Processing Mechanisms:
Pro-NGF is initially synthesized as an inactive precursor, requiring proteolytic cleavage for conversion into mature NGF. The processing of Pro-NGF involves the action of proteases, such as furin, and the formation of distinct protein complexes. The balance between Pro-NGF and mature NGF levels plays a critical role in modulating neuronal function and fate, influencing processes such as neuronal survival, axonal growth, and synaptic plasticity.
Production and Manipulation of Pro-NGF Human Recombinant:
Efficient production methodologies and manipulation strategies are crucial for studying the role of Pro-NGF in neuroregulation and disease pathogenesis. Recombinant protein expression systems, including mammalian cell culture and bacterial expression systems, have been employed to produce functional Pro-NGF human recombinant. Techniques such as mutagenesis, protein purification, and specific inhibitors targeting Pro-NGF processing pathways enable the manipulation of Pro-NGF levels and investigation of its downstream effects.
Implications in Neuroregulation and Disease Pathogenesis:
Pro-NGF human recombinant holds significant potential in understanding the intricate mechanisms underlying neuroregulation and disease pathogenesis. Dysregulation of Pro-NGF processing and altered Pro-NGF/mature NGF ratios have been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and ischemic stroke. Manipulating Pro-NGF levels and the balance between its mature form may offer therapeutic strategies for modulating neurotrophic signaling and promoting neuronal health in these conditions.
Conclusion:
Pro-NGF human recombinant emerges as a key regulator in neuroregulation and disease pathogenesis, offering promising avenues for therapeutic intervention. Enhancing our understanding of Pro-NGF processing mechanisms and its downstream signaling cascades will provide valuable insights into neurodevelopment, neurodegeneration, and potential therapeutic strategies. Targeting Pro-NGF as a therapeutic intervention may hold immense promise in treating neurological disorders and promoting neuronal health.
What is the molecular weight / Mw of ProNGF Protein?
ProNGF Protein has a total Mw of 25kDa.

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

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

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

What is the amino acid sequence of ProNGF Protein?
MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
VCVLSRKAVRRA

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

What is the endotoxin level for ProNGF Protein?
The endotoxin level is minimal, ProNGF 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:

Leukemia Inhibitory Factor Human Recombinant

CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

Product # :

CYT-644

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Shipping Method :

Shipped at Room temp

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Description

Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.

Purity

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

Biological Activity

The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.

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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.
Background
Leukemia Inhibitory Factor (LIF) Background
Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.
LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.
Function and Applications of LIF
LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.
Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.
Structure and Interactions
LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.

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:

Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.

Product # :

CYT-679

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Description

TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 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
MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.
Background
Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.
Introduction:

TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.
Production Process and Characteristics:

TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.
Therapeutic Applications:

TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.
Advantages and Challenges:

The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.
Conclusion:

TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

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:

Sialic Acid Binding Ig Like Lectin 5 Human Recombinant

Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.

Product # :

PRO-2432

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Description

SIGLEC5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 667 amino acids (17-441a.a.) and having a molecular mass of 74.2kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). SIGLEC5 is expressed with a 239 amino acid hIgG-His Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SIGLEC5 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Sialic Acid Binding Ig Like Lectin 5, also known as SIGLEC5 is a member of the immunoglobulin superfamily and SIGLEC family. SIGLEC5 contains of 2 Ig-like C2-type domains and 1 Ig-like V-type domain. In addition, SIGLEC5 is expressed by monocytic/myeloid lineage cells. SIGLEC5 is expressed at high levels in peripheral blood leukocytes, spleen, and at lower levels in lymph node, appendix, pancreas, lung, and thymus.
Synonyms
Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.
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
ADLEKPVYEL QVQKSVTVQE GLCVLVPCSF SYPWRSWYSS PPLYVYWFRD GEIPYYAEVV ATNNPDRRVK PETQGRFRLL GDVQKKNCSL SIGDARMEDT GSYFFRVERG RDVKYSYQQN KLNLEVTALI EKPDIHFLEP LESGRPTRLS CSLPGSCEAG PPLTFSWTGN ALSPLDPETT RSSELTLTPR PEDHGTNLTC QMKRQGAQVT TERTVQLNVS YAPQTITIFR NGIALEILQN TSYLPVLEGQ ALRLLCDAPS NPPAHLSWFQ GSPALNATPI SNTGILELRR VRSAEEGGFT CRAQHPLGFL QIFLNLSVYS LPQLLGPSCS WEAEGLHCRC SFRARPAPSL CWRLEEKPLE GNSSQGSFKV NSSSAGPWAN SSLILHGGLS SDLKVSCKAW NIYGSQSGSV LLLQGRSNLG TGVVPAALLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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:

Adiponectin Mouse Recombinant, Trimeric form

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-247

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.

Source

HEK293 (Human embryonic kidney cell line).

Formulation

Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.

Purity

Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.

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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered white lyophilized (freeze-dried) powder.
Stability
Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.

What is the source or expression system of ADIPONECTIN Protein?
HEK293

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

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

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

What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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:

CD70 Human Recombinant, sf9

CD70 Molecule, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7 , CD27 Ligand, CD27LG, TNFSF7, CD27-L, CD27L, Tumor Necrosis Factor Ligand 8A, Surface Antigen CD70, Ki-24 Antigen, CD70 Antigen, TNLG8A.

Product # :

CYT-953

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Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

TNFSF7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 164 amino acids (39-193 a.a.) and having a molecular mass of 18.2kDa. TNFSF7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFSF7 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
CD70 also known as TNFSF7 is a cytokine which binds to CD27. TNFSF7 takes part in T-cell activation as well as induces the proliferation of costimulated T-cells. Moreover, TNFSF7 enhances the generation of cytolytic T-cells. Among the diseases which are associated with TNFSF7: Include acute myocarditis & Myocarditis.
Synonyms
CD70 Molecule, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7 , CD27 Ligand, CD27LG, TNFSF7, CD27-L, CD27L, Tumor Necrosis Factor Ligand 8A, Surface Antigen CD70, Ki-24 Antigen, CD70 Antigen, TNLG8A.
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
ADPQRFAQAQ QQLPLESLGW DVAELQLNHT GPQQDPRLYW QGGPALGRSF LHGPELDKGQ LRIHRDGIYM VHIQVTLAIC SSTTASRHHP TTLAVGICSP ASRSISLLRL SFHQGCTIAS QRLTPLARGD TLCTNLTGTL LPSRNTDETF FGVQWVRPHH 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:

Mouse Anti Human Dickkopf-Related Protein 3

Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

Product # :

ANT-707

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.
Synonyms
Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human DKK3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human DKK3 protein (22-350 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT103B5AT.
Applications
DKK3 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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
DKK3 antibody was purified from mouse ascitic fluids by protein-A 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:

Geminin, Mouse Anti Human

GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

Product # :

ANT-319

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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Formulation

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

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Introduction
Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. G
Synonyms
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
Immunogen
Anti-human Geminin mAb is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Geminin amino acids 1-209 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P2H7AT.
Applications
Geminin antibody has been tested by ELISA and Western blot 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 analysis is 1:500 ~ 1,000. Recommended starting dilution is 1:500.
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
Geminin 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:

Tumor Necrosis Factor-Alpha Human Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-223

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.

Purity

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

Biological Activity

The Specific Activity is >5.0×10⁷ IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, INS resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.
Background
TNF Alpha Human: An Overview of Its Role and Importance in Immunology
TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.
This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.
Production and Properties
Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.
Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.
Solubility and Usage
The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.
This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.
Storage and Stability
For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.
Biological Role and Implications
TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.
Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.
Mechanism of Action
TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.
Research and Clinical Importance
Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.
Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.
In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.

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:

Vascular Endothelial Growth Factor Equine Recombinant

VEGF-A, VPF, glioma-derived endothelial cell mitogen.

Product # :

CYT-1200

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

VEGF Equine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 2 x 165 amino acids and having a total molecular mass of 38.6 kDa.The VEGF 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.

Biological Activity

The ED₅₀ as determined by HUVEC Proliferation is ≤ 10 ng/mL, corresponding to a specific activity of ≥ 1.0 x 10^5 units/mg.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
VEGF-A, VPF, glioma-derived endothelial cell mitogen.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF 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 VEGF in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPMAEGEHK THEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TAEFNITMQI MRIKPHQSQH IGEMSFLQHS KCECRPKKDK ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR

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:

Interleukin-22 Mouse Recombinant, Pegylated

IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

Product # :

CYT-701

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated solution at 0.65mg/ml containing 0.003mM NaHCO3.

Purity

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

Biological Activity

The ED50 as determined by STAT3 phosphorylation assay in HepG cells. The activity in vitro was found to be ~ 10% compared to the non-pegylated mouse IL22.

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Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10Rβ (previously known as CRF2-4), belonging to the class II cytokine recep
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized pegylated murine IL22 although stable at room temperature for several days, should be stored desiccated below -20°C. Upon reconstitution at 0.1mg/ml pegylated mouse IL22 and up to 2mg/ml, filter and sterilized, the protein can be stored at 4 degrees Celsius for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized pegylated mouse Interleukin -22 in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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:

Thymopentin

Product # :

HOR-241

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
purity
biological activity
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Description

Thymopentin has a molecular formula of C30H49N9O9, Arg-Lys-Asp-Val-Tyr-OH having an Mw of 679.8 Dalton.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

What is the molecular weight/Mw of THYMOPENTIN Protein? THYMOPENTIN Protein has a total Mw of 0.67kDa. What is the Purity of THYMOPENTIN Protein? THYMOPENTIN Protein is >99% pure as determined by SDS-PAGE. What is the Biological Activity of THYMOPENTIN Protein? The biological functionality of THYMOPENTIN Protein will be determined in the future. What applications can THYMOPENTIN Protein be used in? THYMOPENTIN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for THYMOPENTIN Protein? The endotoxin level is minimal, THYMOPENTIN Protein was purified using conventional chromatography techniques.

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Introduction
Thymopentin, also known as TP-5, is a synthetic pentapeptide which is the active site of the naturally occurring hormone thymopoietin with immunomodulating properties (corresponding to the amino acids 32-36 of thymopoietin). Thymopentin enhances the production of thymic T cells and may help restore immunocompetence in immunosuppressed subjects. This agent also augments the effects of ionizing radiation by arresting cancer cells in the G2/M phase of the cell cycle.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymopentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TP-5 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 Thymopentin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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:

EGF Like Domain Multiple 6 Human Recombinant

EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.

Product # :

CYT-974

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

EGF Like Domain Multiple 6 Human Recombinant produced in HEK cells is a polypeptide chain starting at amino acid Asn at position 22 to amino acid Arg at position 363, fused to an FC, 6 x His-tag at C-terminus, containing a total of 348 amino acids and having a predicted molecular mass of 40-55kDa. The EGFL6 is purified by proprietary chromatographic techniques.

Source

HEK (Human embryonic kidney cells).

Formulation

The EGFL6 protein was lyophilized from a 0.2µm filtered solution in 20mM MES and 500mM NaCl, pH 6.0 with 5% Trehalose.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

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Introduction
Epidermal Growth Factorlike Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.
Synonyms
EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EGFL6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGFL6 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 EGFL6 in sterile PBS at 500µg/ml, which can then be further diluted to other aqueous solutions.
Background
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential
Abstract:
This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.
Protein Expression and Purification:
The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.
Cellular Signaling Pathways and Responses:
In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Structural Modeling:
Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.
Therapeutic Implications and Future Prospects:
EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.
Challenges and Future Directions:
Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.
Conclusion:
A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGFL6 HUMAN Protein?
EGFL6 HUMAN Protein has a total Mw of 40-55kDa.

What is the source or expression system of EGFL6 HUMAN Protein?
HEK (Human embryonic kidney cells).

What is the Purity of EGFL6 HUMAN Protein?
EGFL6 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EGFL6 HUMAN Protein?
EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

What is the amino acid sequence of EGFL6 HUMAN Protein?
EGFL6 HUMAN Protein is composed from 348 amino acids.

What applications can EGFL6 HUMAN Protein be used in?
EGFL6 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGFL6 HUMAN Protein?
The endotoxin level is minimal, EGFL6 HUMAN 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:

Cytomegalo Virus Pp65 (UL83) Recombinant

Product # :

CMV-215

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

The E.Coli derived 52.2 kDa recombinant protein contains the CMV Pp65 (UL83) immunodominant regions, 297-510 amino acids. Recombinant CMV-Pp65 is fused to a 26 kDa GST tag.

Source

Escherichia Coli.

Formulation

CMV PP65 protein solution is supplied in PBS.

Purity

CMV Pp65 protein is >90% pure as determined by SDS-PAGE.

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Introduction
CMV belongs to the Betaherpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.
Stability
CMV Pp65 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
CMV Pp65 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.
Specificity
Strongly reacts with human CMV positive serum.
Purification Method
CMV Pp65 was purified by proprietary chromatographic technique.

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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