Search: 343 results found for "Mediator Complex"

Description:

Proteasome Subunit Alpha Type 5 Human Recombinant

Proteasome subunit alpha type-5, Macropain zeta chain, Multicatalytic endopeptidase complex zeta chain, Proteasome zeta chain, PSMA5, PSC5, ZETA.

Product # :

ENZ-213

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PSMA5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-241) and having a molecular mass of 30.5kDa.PSMA5 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PSMA5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Proteasome subunit alpha type-5 (PSMA5) is a member of the peptidase T1A family. The proteasome is a multicatalytic proteinase complex which is distinguished by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. PSMA5 interacts with PLK1. The PSMA5 peptidase has a very wide-ranging specificity for cleavage of peptide bonds.
Synonyms
Proteasome subunit alpha type-5, Macropain zeta chain, Multicatalytic endopeptidase complex zeta chain, Proteasome zeta chain, PSMA5, PSC5, ZETA.
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 KDRWGSMFLT RSEYDRGVNT FSPEGRLFQV EYAIEAIKLG STAIGIQTSE GVCLAVEKRI TSPLMEPSSI EKIVEIDAHI GCAMSGLIAD AKTLIDKARV ETQNHWFTYN ETMTVESVTQ AVSNLALQFG EEDADPGAMS RPFGVALLFG GVDEKGPQLF HMDPSGTFVQ CDARAIGSAS EGAQSSLQEV YHKSMTLKEA IKSSLIILKQ VMEEKLNATN IELATVQPGQ NFHMFTKEEL EEVIKDI.

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:

Mitochondrial Trans-2-Enoyl-CoA Reductase Human Recombinant

NRBF1, CGI-63, FASN2B, EC 1.3.1.38, MECR, Mitochondrial Trans-2-Enoyl-CoA Reductase.

Product # :

ENZ-533

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

MECR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (54-373 a.a.) and having a molecular mass of 49.8 kDa. The MECR is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MECR Human solution containing 20mM Trsi pH-8, 0.2M NaCl, 5mM DTT & 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
MECR catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH dependent manner with preference to medium chain length substrate. MECR protein takes part in the mitochondrial synthesis of fatty acids.
Synonyms
NRBF1, CGI-63, FASN2B, EC 1.3.1.38, MECR, Mitochondrial Trans-2-Enoyl-CoA Reductase.
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 MPAKVVELKN LELAAVRGSD VRVKMLAAPI NPSDINMIQG NYGLLPELPA VGGNEGVAQV VAVGSNVTGL KPGDWVIPAN AGLGTWRTEA VFSEEALIQV PSDIPLQSAA TLGVNPCTAY RMLMDFEQLQ PGDSVIQNAS NSGVGQAVIQ IAAALGLRTI NVVRDRPDIQ KLSDRLKSLG AEHVITEEEL RRPEMKNFFK DMPQPRLALN CVGGKSSTEL LRQLARGGTM VTYGGMAKQP VVASVSLLIF KDLKLRGFWL SQWKKDHSPD QFKELILTLC DLIRRGQLTA PACSQVPLQD YQSALEASMK PFISSKQILT M.

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:

Thymulin

Product # :

HOR-047

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
formulation
purity
More Info
Citations

Description

Thymulin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 858 Dalton and a Molecular formula of C33H54N12O15.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymulin 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 Thymulin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.
Background
Thymulin, a nonapeptide hormone, is produced primarily by the thymus gland and has been recognized for its pivotal role in the immune system. It plays a significant role in the maturation and differentiation of T lymphocytes, which are crucial for immune function. Beyond its immune-related functions, research has increasingly unveiled the diverse physiological roles of thymulin. This study aims to comprehensively investigate thymulin, shedding light on its immunological functions and exploring its potential applications in various aspects of health and medicine.
The primary objective of this research is to elucidate the mechanisms underlying thymulin's role in immune regulation. In vitro and in vivo experiments will be conducted to explore thymulin's interactions with immune cells, its impact on T cell development and function, and its potential modulation of immune responses. Understanding these mechanisms is fundamental for harnessing thymulin's immunomodulatory properties.
The second objective is to assess the clinical relevance of thymulin in immune-related disorders. Clinical trials and studies involving individuals with autoimmune diseases, immunodeficiencies, and age-related immune decline will be conducted to evaluate the potential therapeutic applications of thymulin. These investigations may offer insights into the use of thymulin as an immunomodulatory agent in various clinical settings.
The third objective is to explore the broader implications of thymulin in health and medicine. Research will investigate its potential roles in areas beyond immunology, such as neuroprotection, wound healing, and tissue regeneration. Understanding the multifaceted properties of thymulin may open new avenues for therapeutic interventions in various medical specialties.
By delving into the diverse functions of thymulin, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may have implications for the development of innovative approaches in immunology and healthcare, ultimately benefiting patients affected by immune-related disorders and other medical conditions.
What is the molecular weight/Mw of THYMALIN Protein?
THYMALIN Protein has a total Mw of 0.85kDa.

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

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

What is the amino acid sequence of THYMALIN Protein?
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.

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

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

Collapsin Response Mediator Protein-1 Mouse Recombinant

Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.

Product # :

PRO-2521

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CRMP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (1-572 a.a) and having a molecular mass of 64.8kDa.CRMP1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CRMP1 protein solution (0.25mg/ml) contains 40% glycerol, 20mM Tris-HCl (pH 8.5), 0.2M NaCl & 0.1mM PMSF.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation as well as axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The X-ray crystal structure of murine CRMP1 was determined at 2.1 resolution and demonstrates that CRMP1 is a bilobed ‘lung-shaped’ protein forming a tetrameric assembly.
Synonyms
Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.
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
MGSSHHHHHH SSGLVPRGSH MGSEFMSHQG KKSIPHITSD RLLIRGGRII NDDQSFYADV YLEDGLIKQI GENLIVPGGV KTIEANGRMV IPGGIDVNTY LQKPSQGMTS ADDFFQGTKA ALAGGTTMII DHVVPEPGSS LLTSFEKWHE AADTKSCCDY SLHVDITSWY DGVREELEVL VQDKGVNSFQ VYMAYKDLYQ MSDSQLYEAF TFLKGLGAVI LVHAENGDLI AQEQKRILEM GITGPEGHAL SRPEELEAEA VFRAIAIAGR INCPVYITKV MSKSAADIIA LARKKGPLVF GEPIAASLGT DGTHYWSKNW AKAAAFVTSP PLSPDPTTPD YLTSLLACGD LQVTGSGHCP YSTAQKAVGK DNFTLIPEGV NGIEERMTVV WDKAVATGKM DENQFVAVTS TNAAKIFNLY PRKGRIAVGS DADVVIWDPD KMKTITAKSH KSTVEYNIFE GMECHGSPLV VISQGKIVFE DGNISVSKGM GRFIPRKPFP EHLYQRVRIR SKVFGLHSVS RGMYDGPVYE VPATPKHAAP APSAKSSPSK HQPPPIRNLH QSNFSLSGAQ IDDNNPRRTG HRIVAPPGGR SNITSLG.

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-28A Human Recombinant, His Tag

Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.

Product # :

CYT-813

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

IL 28A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (26-200 a.a.) and having a molecular mass of 22.1kDa. IL 28A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 28A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
IL-28A is distantly related to type I interferons and the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
Synonyms
Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
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 MGSVPVARLH GALPDARGCH IAQFKSLSPQ ELQAFKRAKD ALEESLLLKD CRCHSRLFPR TWDLRQLQVR ERPMALEAEL ALTLKVLEAT ADTDPALVDV LDQPLHTLHH ILSQFRACIQ PQPTAGPRTR GRLHHWLYRL QEAPKKESPG CLEASVTFNL FRLLTRDLNC VASGDLCV .

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 28B Human Recombinant

Lambda 3, IL28B, Interleukin 28B (IFN, Lambda 3), Cytokine Zcyto22, Interleukin-28B, Interleukin-28C, IFN-Lambda-3, IL-28B, IL-28C, IL28C, Lambda 4, Interleukin 28B, Interleukin 28C, IFN-Lambda-4, ZCYTO22, IFNL3.

Product # :

CYT-893

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

IL 28B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (22-196 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 181 amino acids and having a molecular mass of 20.4kDa.IL 28B shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL 28B protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol, 1mM EDTA and 0.1mM PMSF.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
IL-28B is a cytokine remotely related to type I IFNs and the IL-10 family. Interleukin-28B, interleukin 28A (IL28A), and interleukin 29 (IL29) are 3 closely related cytokine genes which form a cytokine gene cluster on a chromosomal region mapped to 19q13. Expression of the cytokines encoded by these 3 genes can be induced by viral infection. All 3 cytokines interact with a heterodimeric class II cytokine receptor which consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha (IL28RA).
Synonyms
Lambda 3, IL28B, Interleukin 28B (IFN, Lambda 3), Cytokine Zcyto22, Interleukin-28B, Interleukin-28C, IFN-Lambda-3, IL-28B, IL-28C, IL28C, Lambda 4, Interleukin 28B, Interleukin 28C, IFN-Lambda-4, ZCYTO22, IFNL3.
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
VPVARLRGAL PDARGCHIAQ FKSLSPQELQ AFKRAKDALE ESLLLKDCKC RSRLFPRTWD LRQLQVRERP VALEAELALT LKVLEATADT DPALGDVLDQ PLHTLHHILS QLRACIQPQP TAGPRTRGRL HHWLHRLQEA PKKESPGCLE ASVTFNLFRL LTRDLNCVAS GDLCVHHHHHH.

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:

Dihydrolipoamide S-Succinyltransferase Human Recombinant

dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.

Product # :

ENZ-083

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

DLST is a Full-length cDNA coding for the mature form of the human OGDC-E2 protein having a molecular mass of 42,301 Dalton (pH 6.3).DLST protein is fused to a hexa-histidine purification tag.

Source

Sf9 insect cells.

Formulation

DLST (0.74mg/ml) is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

Purity

DLST purity was found to be greater than 75% as determined by SDS-PAGE.

More Info

Introduction
DLST catalyzes the general transformation of 2-oxoglutarate to succinyl-CoA and CO(2). DLST holds multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Synonyms
dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.
Stability
Store DLST at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. DLST binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.
coating concentration
0.4-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.
Applications
Western blot with anti-M2-Antigen autoantibody-positive patient sera or monoclonal
anti-hexa-His-tag antibody.

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:

Histidine NADH Dehydrogenase Fe-S Protein 6 Human Recombinant

NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa (NADH-Coenzyme Q Reductase), Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, CI13KDA.

Product # :

ENZ-725

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa (NADH-Coenzyme Q Reductase), Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, CI13KDA.

Source

Escherichia Coli.

Formulation

The NDUFS6 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
NADH Dehydrogenase Fe-S Protein 6 (NDUFS6) is a subunit of the NADH: ubiquinone oxidoreductase (complex I), which is the 1st enzyme complex in the electron transport chain of the mitochondria. This complex operates in the transfer of electrons from NADH to the respiratory chain. NDUFS6 is one of seven subunits in the iron-sulfur protein segment. DNA alterations in NDUFS6 are the cause for mitochondrial complex I deficiency, a disease which results in an extensive assortment of clinical disorders, like adult-onset neurodegenerative disorders and neonatal disease.
Synonyms
NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa (NADH-Coenzyme Q Reductase), Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, CI13KDA.
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
MGSSHHHHHH SSGLVPRGSH MGSFGVRVSP TGEKVTHTGQ VYDDKDYRRI RFVGRQKEVN ENFAIDLIAE QPVSEVETRV IACDGGGGAL GHPKVYINLD KETKTGTCGY CGLQFRQHHH

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-20 Human Recombinant

IL10D, ZCYTO10, IL-20, MGC96907, Four alpha helix cytokine Zcyto10.

Product # :

CYT-347

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Interleukin-20 Human Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 2 x 153 amino acids and having a total molecular mass of 35,212 Dalton. The IL-20 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized carrier free.

Purity

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

Biological Activity

The Biological Activity was determined by measuring the dose dependent activation of STAT3 in human epidermal keratinocytes (HEKa cells).Significant STAT3 activation is observed with 100 ng/mL of recombinant human IL-20 corresponding to a Specific Activity of 10,000IU/mg.

More Info

Introduction
IL20 is a cytokine structurally related to interleukin 10 (IL10). IL20 cytokine has been shown to transduce its signal through signal transducer and activator of transcription 3 (STAT3) in keratinocytes. A specific receptor for this cytokine is found to be expressed in skin and upregulated dramatically in psoriatic skin, suggesting a role for this protein in epidermal function and psoriasis.
Synonyms
IL10D, ZCYTO10, IL-20, MGC96907, Four alpha helix cytokine Zcyto10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL20 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 Interleukin -20 in sterile 18MΩ-cm H2O at a concentration of 0.5mg/ml or less.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Lys-Thr-Leu.

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:

Prolactin Rabbit Soluble Receptor Recombinant

PRL-R.

Product # :

CYT-268

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Prolactin Receptor Rabbit Extra Celleular Domain Recombinant ?produced in E.Coli is a non-glycosylated, Polypeptide chain containing 207 amino acids and having a molecular mass of 23972 Dalton. The Prolactin Receptor is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

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

Biological Activity

Activity is determined by the dose-dependant inhibition of Prolactin-stimuled proliferation of Nb2 cells and by high affinity binding of oPLR and other lactogenic hormones. Refs:
1) Bignon et al. (1994) JBC 269; 3318-24
2) Gertler et al. (1996) JBC 271; 24482-91.

More Info

Introduction
Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
Synonyms
PRL-R.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PRL-R although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin Receptor 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 PRL-R 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 Gly-Lys-Pro-Phe-Ile.
Protein content
UV spectroscopy at 280 nm using the absorbency value of 2.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENEcomputer 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:

CCR4-NOT Transcription Complex, Subunit 7 Mouse Recombinant

CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.

Product # :

PRO-908

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CNOT7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-248 a.a) and having a molecular mass of 31.1kDa.CNOT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CNOT7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
CCR4-Not transcription complex, subunit 7 (CNOT7) is a ubiquitous transcription factor. CNOT7 is a component of the CCR4 complex which functions as a general transcription regulation complex. Furthermore, CNOT7 binds to an anti-proliferative protein, BTG1 (B-cell translocation protein 1), which negatively regulates cell proliferation.
Synonyms
CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.
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 MGSMPAATVD HSQRICEVWA CNLDEEMKKI RQVIRKYNYV AMDTEFPGVV ARPIGEFRSN ADYQYQLLRC NVDLLKIIQL GLTFMNEQGE YPPGTSTWQF NFKFNLTEDM YAQDSIELLT TSGIQFKKHE EEGIETQYFA ELLMTSGVVL CEGVKWLSFH SGYDFGYLIK ILTNSNLPEE ELDFFEILRL FFPVIYDVKY LMKSCKNLKM FFEDHIDDAK YCGHLYGLGS GSSYVQNGTG NAYEEEASKQ S.

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 Migration Inhibitory Factor, Mouse Anti Human

Phenylpyruvate tautomerase, Glycosylation- inhibiting factor, GIF, MMIF, MIF.

Product # :

ANT-311

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info
Citations

Formulation

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

More Info

Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Phenylpyruvate tautomerase, Glycosylation- inhibiting factor, GIF, MMIF, MIF.
Immunogen
Anti-human MIF mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human MIF amino acids 1-114 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P4E4AT.
Applications
MIF 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
MIF 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:

Leptin Quadruple Antagonist Pegylated Human Recombinant

Product # :

CYT-1251

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 98.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.

More Info

Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature 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 Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Background
Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. 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:

Aminoacyl tRNA Synthetase Complex-Interacting Multifunctional Protein 1 Human Recombinant

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.

Product # :

CYT-021

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page
Citations

Description

AIMP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 356 amino acids (1-336 a.a.) and having a molecular mass of 39.2kDa (Molecular size on SDS-PAGE will appear higher). The AIMP1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The AIMP1 solution (0.25mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

More Info

Introduction
AIMP1 (EMPA2 or p43) is a cytokine that is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of the AIMP1 cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. Furthermore, AIMP1 is involved in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
Synonyms
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
Background
What is the molecular weight/Mw of AIMP1 HUMAN Protein?
AIMP1 HUMAN Protein has a total Mw of 39.2kDa.

What is the source or expression system of AIMP1 HUMAN Protein?
Escherichia Coli.

What is the Purity of AIMP1 HUMAN Protein?
AIMP1 HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of AIMP1 HUMAN Protein?
The biological functionality of AIMP1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of AIMP1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

What applications can AIMP1 HUMAN Protein be used in?
AIMP1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AIMP1 HUMAN Protein?
The endotoxin level is minimal, AIMP1 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:

Bone Morphogenetic Protein-4 Human Recombinant

BMP4, ZYME, BMP2B, BMP2B1.

Product # :

CYT-361

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.

Purity

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

More Info

Introduction
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.
Synonyms
BMP4, ZYME, BMP2B, BMP2B1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
Background
What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant
As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.
Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.
Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!
How Does Bone Morphogenetic Protein-4 (BMP-4) Work?
Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.
The Role of BMP-4
This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.
However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:
- Embryonic development
- Wound healing
- Bone remodeling
- Immune response modulation
- Tissue repair
- Cardiac development and function
What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?
To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.
As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.
More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:
- Cancer therapy
- Development of engineered tissues and organs
- Bone regeneration for the treatment of osteoporosis and nonunion fractures
- Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
- Promotion of tissue repair and regeneration
Final Thoughts BMP-4
Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.
However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.
What is the molecular weight/Mw of BMP4 Protein?
BMP4 Protein has a total Mw of 13kDa.

What is the source or expression system of BMP4 Protein?
Escherichia Coli.

What is the Purity of BMP4 Protein?
BMP4 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP4 Protein?
The biological functionality of BMP4 Protein will be determined in the future.

What is the amino acid sequence of BMP4 Protein?
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

What applications can BMP4 Protein be used in?
BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP4 Protein?
The endotoxin level is minimal, BMP4 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:

Proteasome Subunit Alpha Type 4 Human Recombinant

Proteasome subunit alpha type-4, Macropain subunit C9, Multicatalytic endopeptidase complex subunit C9, Proteasome component C9, Proteasome subunit L, PSMA4, HC9, PSC9, HsT17706.

Product # :

ENZ-222

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PSMA4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-261) and having a molecular mass of 32kDa.PSMA4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PSMA4 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Proteasome subunit alpha type 4 (PSMA4) belongs to the peptidase T1A family, which is a 20S core alpha subunit. The proteasome is a multicatalytic proteinase complex with an extremely ordered ring-shaped 20S core structure. The core structure is comprised of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. PSMA4 is dispersed throughout eukaryotic cells at a high concentration and cleaves peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.
Synonyms
Proteasome subunit alpha type-4, Macropain subunit C9, Multicatalytic endopeptidase complex subunit C9, Proteasome component C9, Proteasome subunit L, PSMA4, HC9, PSC9, HsT17706.
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 MGSHMSRRYD SRTTIFSPEG RLYQVEYAME AIGHAGTCLG ILANDGVLLA AERRNIHKLL DEVFFSEKIY KLNEDMACSV AGITSDANVL TNELRLIAQR YLLQYQEPIP CEQLVTALCD IKQAYTQFGG KRPFGVSLLY IGWDKHYGFQ LYQSDPSGNY GGWKATCIGN NSAAAVSMLK QDYKEGEMTL KSALALAIKV LNKTMDVSKL SAEKVEIATL TRENGKTVIR VLKQKEVEQL IKKHEEEEAK AEREKKEKEQ KEKDK.

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 Migration Inhibitory Factor Rat Recombinant

Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

Product # :

CYT-193

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa. The MIF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.

Purity

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

More Info

Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.

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

Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

Product # :

CYT-308

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 159 amino acids and having a total molecular mass of 37.1 KD. MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MCSF protein was lyophilized with 10mM sodium Phosphate, pH-8.0 & 50mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependent stimulation of the proliferation of murine M-NFS-60 indicator cells was found to be 1.15ng/ml corresponding to a specific activity of 8.7x10⁵ Units/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. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCSF 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 MCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ GHERQSEGS.
Background
M-CSF (Macrophage-Colony Stimulating Factor) Human Recombinant: Unraveling Its Role in Macrophage Biology and Beyond
Abstract:
M-CSF (Macrophage-Colony Stimulating Factor), also known as Lanimostim, MCSF, or MGC31930, is a crucial growth factor that regulates the development, proliferation, and function of macrophages.
This research paper aims to provide a comprehensive analysis of the molecular characteristics, signaling pathways, and diverse physiological functions of M-CSF. Additionally, it explores the therapeutic implications of M-CSF in various diseases and disorders.
Synonyms such as Lanimostim, MCSF, and MGC31930 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
1. M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a growth factor that plays a critical role in the regulation of macrophage biology. This section introduces M-CSF and its synonyms, highlighting their significance and relevance in scientific research.
Molecular Characteristics of M-CSF:
1. This section explores the molecular characteristics of M-CSF, including its primary amino acid sequence, protein structure, and post-translational modifications. The importance of these factors in determining M-CSF's biological activity and receptor binding is discussed.
Signaling Pathways Activated by M-CSF:
1. M-CSF activates specific signaling pathways upon binding to its receptor, leading to diverse cellular responses. This section focuses on the activation of the MAPK/ERK and PI3K/Akt pathways. The downstream effectors and transcriptional regulators involved in mediating M-CSF's cellular responses are also discussed.
Physiological Functions of M-CSF:
1. M-CSF plays critical roles in various physiological processes, particularly in macrophage development, survival, polarization, and immune regulation. This section provides an in-depth analysis of M-CSF's contributions to these processes, emphasizing its role in hematopoiesis, tissue homeostasis, wound healing, and host defense.
Therapeutic Implications of M-CSF:
1. The unique properties of M-CSF make it a promising therapeutic candidate for various diseases and disorders. This section discusses the potential applications of M-CSF in immunotherapy, tissue regeneration, cancer treatment, and autoimmune diseases. The challenges and future directions in utilizing M-CSF as a therapeutic agent are also explored.
M-CSF in Disease Pathogenesis:
1. M-CSF dysregulation is implicated in the pathogenesis of several diseases, including cancer, inflammation, and bone disorders. This section examines the role of M-CSF in promoting tumor progression, macrophage-mediated inflammation, osteoclast differentiation, and metabolic diseases. The therapeutic implications and targeting of M-CSF in disease management are also discussed.
Conclusion:
1. M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a critical growth factor involved in macrophage biology and disease pathogenesis. Understanding the molecular characteristics, signaling pathways, and physiological functions of M-CSF contributes to the exploration of its therapeutic potential in various disorders.

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:

Hepatocyte Growth Factor Human Recombinant, HEK

Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.

Product # :

CYT-090

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

HGF Human Recombinant produced in HEK cells is a glycosylated disulfide-linked heterodimer, containing 697 a.a. (Gln-32 to Ser-728) having a total molecular weight of 80kDa. The HGF is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The HGF was lyophilized from a solution (1mg/ml) containing 10mM Sodium phosphate, 150mM NaCl, 0.01% Tween 80 and 100mM L-Arginine, pH 6.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC₅₀for this effect is typically 20-40ng/ml.

More Info

Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized HGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF 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 Hepatocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein has a total Mw of 80kDa.

What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEK.
What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC50 for this effect is typically 20-40ng/ml.
What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728

What applications can HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein be used in?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN,HEK 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:

Centromere Protein-U Human Recombinant

Centromere Protein U, MLF1IP, Polo-Box-Interacting Protein 1, MLF1 Interacting Protein, Centromere Protein Of 50 KDa, Interphase Centromere Complex Protein 24, KLIP1, PBIP1, KSHV Latent Nuclear Antigen-Interacting Protein 1, MLF1-Interacting Protein, CENP50, CENPU50, KSHV Latent Nuclear Antigen Interacting Protein 1, CENP-50, CENP-U, ICEN24.

Product # :

PRO-1824

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CENPU Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (147-418a.a) and having a molecular mass of 33.7kDa.CENPU is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CENPU protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
Centromere Protein U, also known as CENPU is a specialized chromatin domain, present throughout the cell cycle. CENPU performs as a platform on which the transient assembly of the kinetochore takes place during mitosis. CENPU plays a major role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein is responsible for the first recruitment and maintenance of the kinetochore PLK1 population until its degradation. CENPU is also implicated in transcriptional repression.
Synonyms
Centromere Protein U, MLF1IP, Polo-Box-Interacting Protein 1, MLF1 Interacting Protein, Centromere Protein Of 50 KDa, Interphase Centromere Complex Protein 24, KLIP1, PBIP1, KSHV Latent Nuclear Antigen-Interacting Protein 1, MLF1-Interacting Protein, CENP50, CENPU50, KSHV Latent Nuclear Antigen Interacting Protein 1, CENP-50, CENP-U, ICEN24.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTRRKVKS AEKISTQRHE VIRTTASSEL SEKPAESVTS KKTGPLSAQP SVEKENLAIE SQSKTQKKGK ISHDKRKKSR SKAIGSDTSD IVHIWCPEGM KTSDIKELNI VLPEFEKTHL EHQQRIESKV CKAAIATFYV NVKEQFIKML KESQMLTNLK RKNAKMISDI EKKRQRMIEV QDELLRLEPQ LKQLQTKYDE LKERKSSLRN AAYFLSNLKQ LYQDYSDVQA QEPNVKETYD SSSLPALLFK ARTLLGAESH LRNINHQLEK LLDQG

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:

Tubulin Polyglutamylase Complex Subunit 2 Human Recombinant

Tubulin polyglutamylase complex subunit 2, C18orf10; HMFN0601, HsT3006, L17, PGs2, TPGS2.

Product # :

PRO-1668

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

TPGS2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300) and having a molecular mass of 35.7kDa.TPGS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TPGS2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Tubulin Polyglutamylase Complex Subunit 2 (TPGS2) is a component of the neuronal polyglutamylase complex, which takes part in post-translational addition of glutamate residues to C-terminal tubulin tails. Alternatively spliced transcript variants encoding multiple isoforms have been monitored for TPGS2.
Synonyms
Tubulin polyglutamylase complex subunit 2, C18orf10; HMFN0601, HsT3006, L17, PGs2, TPGS2.
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 MGSMEEEASS PGLGCSKPHL EKLTLGITRI LESSPGVTEV TIIEKPPAER HMISSWEQKN NCVMPEDVKN FYLMTNGFHM TWSVKLDEHI IPLGSMAINS ISKLTQLTQS SMYSLPNAPT LADLEDDTHE ASDDQPEKPH FDSRSVIFEL DSCNGSGKVC LVYKSGKPAL AEDTEIWFLD RALYWHFLTD TFTAYYRLLI THLGLPQWQY AFTSYGISPQ AKQWFSMYKP ITYNTNLLTE ETDSFVNKLD PSKVFKSKNK IVIPKKKGPV QPAGGQKGPS GPSGPSTSST SKSSSGSGNP TRK.

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:

CD30 Ligand Human Recombinant, Sf9

Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.

Product # :

CYT-954

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

TNFSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 181 amino acids (63-234a.a.) and having a molecular mass of 20.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). TNFSF8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.
Synonyms
Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.
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
ADPQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSDHHHHH H.

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-13 Human Recombinant

CLG3, MANDP1, Matrix metalloproteinase-13, MMP-13, MMP13.

Product # :

ENZ-317

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

MMP-13 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (104-471 a.a.) and having a molecular mass of 44.7 kDa. MMP-13 is fused to a 23 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MMP-13 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
Matrix Metalloproteinase-13 (MMP-13) is an enzyme that is a member of the MMP extracellular protease family. Extracellular protease enzymes, by virtue of their broad substrate specificities1, play a role in both normal and disease states of tissue proliferation. Among the targets of MMP-13 are collagen, gelatin, entactin, pro-TNF-a, and chemokine SDF-11-4.
MMP-13 is found in its latent form as a 52-56 kDa glycosylated proenzyme. Upon cleavage the 22-46 kDa5 MMP-1 becomes active in extracellular matrix remodeling.
Because of the prominent role that MMP-1 plays in cell migration and metastasis, it is an important target for inhibition screening.
Synonyms
CLG3, MANDP1, Matrix metalloproteinase-13, MMP-13, MMP13.
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
MGSSHHHHHH SSGLVPRGSH MGSYNVFPRT LKWSKMNLTY RIVNYTPDMT HSEVEKAFKK AFKVWSDVTP LNFTRLHDGI ADIMISFGIK EHGDFYPFDG PSGLLAHAFP PGPNYGGDAH FDDDETWTSS SKGYNLFLVA AHEFGHSLGL DHSKDPGALM FPIYTYTGKS HFMLPDDDVQ GIQSLYGPGD EDPNPKHPKT PDKCDPSLSL DAITSLRGET MIFKDRFFWR LHPQQVDAEL FLTKSFWPEL PNRIDAAYEH PSHDLIFIFR GRKFWALNGY DILEGYPKKI SELGLPKEVK KISAAVHFED TGKTLLFSGN QVWRYDDTNH IMDKDYPRLI EEDFPGIGDK VDAVYEKNGY IYFFNGPIQF EYSIWSNRIV RVMPANSILW C.

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 Anti Human

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

Product # :

ANT-232

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info
Citations

Formulation

containing PBS, pH-7.4, & 0.1% Sodium Azide

More Info

Introduction
Human Adiponectin is a secreted protein expressed exclusively in differentiated adipocyte (adipokine). Adiponectin contains a modular structure comprising an N-terminal collagenous domain followed by a C-terminal globular domain. APM-1 plays a role in various physiological processes such as energy homeostasis and obesity. Plasma levels of adiponectin are reduced in obese humans, and decreased levels are associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Sterile Filtered solution.
Immunogen
Anti-human adiponectin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human adiponectin amino acids 15-244 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
P1G12AT.
Applications
Adiponectin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Recommended dilution range for Western blot analysis is 1:250 ~ 1:1,000. The antibody has the specificity against globular domain of adiponectin. 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
Adiponectin 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.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info