Search: 1000 results found for "Nucleobindin"

Description:

Ubiquitin Domain Containing 2 Human Recombinant

Ubiquitin domain containing protein 2, Dendritic cell-derived ubiquitin-like protein, Ubiquitin-like protein SB72, DCUBP, MGC30022.

Product # :

PRO-1203

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Description

UBTD2 Human Recombinant produced in E. coli is a single polypeptide chain containing 257 amino acids (1-234) and having a molecular mass of 28.6 kDa.UBTD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The UBTD2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
UBTD2 is an ubiquitin (Ub) domain-containing protein, originally recognized in dendritic cells, that takes part in ubiquitination pathway. Ubiquitin is the best understood post-translation modifier; however, there is a growing family of ubiquitin-like proteins (UBLs) who change cellular targets in a pathway. UbL proteins take part in a variation of cellular courses, like DNA repair, protein sorting, protein degradation, cell division, apoptosis and autophagy.
Synonyms
Ubiquitin domain containing protein 2, Dendritic cell-derived ubiquitin-like protein, Ubiquitin-like protein SB72, DCUBP, MGC30022.
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 MGSMGGCVGA QHDSSGSLNE NSEGTGVALG RNQPLKKEKP KWKSDYPMTD GQLRSKRDEF WDTAPAFEGR KEIWDALKAA AHAFESNDHE LAQAIIDGAN ITLPHGALTE CYDELGNRYQ LPVYCLAPPI NMIEEKSDIE TLDIPEPPPN SGYECQLRLR LSTGKDLKLV VRSTDTVFHM KRRLHAAEGV EPGSQRWFFS GRPLTDKMKF EELKIPKDYV VQVIVSQPVQ NPTPVEN

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:

Activin-A Human Recombinant, CHO

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-1258

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Description

Activin-A Human Recombinant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 26.0kDa. The Active form Activin-A is purified by standard chromatographic techniques.

Source

CHO cells.

Formulation

Human Activin-A was lyophilized from a concentrated filtered solution in 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 10⁵ units/mg.

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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-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
Human INHBA protein should be reconstituted in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C. Further dilutions should be made in appropriate buffered solutions.
Amino Acid Sequence
GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS.
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26 kDa.
What is the source or expression system of Activin A Protein?
CHO Cells.

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

What is the Biological Activity of Activin A Protein?
Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 105 units/mg.

What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of ACTIVIN A Protein?
GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS

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

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:

Creatine Kinase MB Human Recombinant

CKMB, CK-MB

Product # :

CKI-286

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Description

Recombinant Human Creatine Kinase MB produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.The CKMB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein solution contains 50mM Tris-HCL, 5mM B-mercaptoethanol, 1mM EDTA, 5mM disodium Succinate, Ph 8.0 and 50% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
Physical Appearance
Sterile Filtered colorless liquid formulation.
Stability
CKMB although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.

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:

Natural anti-proliferative protein, Mouse-Anti Human

Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

Product # :

ANT-170

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Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human NAP-2.
Ig Subclass
Mouse IgG1.
Clone
NYRhNAP-2.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Note
This antibody will bind very well to protein A in a buffer (PBS) containing high salt concentration (3M Nacl).
Titer
In direct ELISA, using alkaline phosphatase goat anti-mouse Ig (Jackson Laboratories) 1:10,000 dilution will yield 0.5 O.D within 10 minutes.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
ion exchange.

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-12 p75, Rat Anti-Mouse

Product # :

ANT-209

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Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of interferon gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Murine IL-12 p75.
Ig Subclass
Rat IgG2b.
Clone
NYRmIL-12p75.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Note
This antibody recognizes the entire IL-12 molecule and has no reactivity to denatured p40 or p35.
Titer
By direct ELISA, 1:5,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Rat Anti Mouse Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion exchange.

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:

Epstein Barr Virus Induced 3 Mouse Recombinant

IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.

Product # :

CYT-621

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Quantity :

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Description

EBI3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 22.9kDa. The Murine EBI3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EBI3 was lyophilized from 10mM Sodium Citrate pH-3.

Purity

Greater than 90% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
Synonyms
IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 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 EBI3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.
Background
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 22.9kDa.

What is the source or expression system of EBI3 Protein?
Escherichia Coli.

What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of EBI3 Protein?
The biological functionality of EBI3 Protein will be determined in the future.

What is the amino acid sequence of EBI3 Protein?
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.

What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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:

Growth and Differentiation factor 11 Human Recombinant, His Tag

Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.

Product # :

CYT-887

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Shipped with Ice Packs

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Description

GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
Synonyms
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
Background
What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.

What is the source or expression system of GDF11 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF11 HUMAN, HIS Protein?
The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.

What applications can GDF11 HUMAN, HIS Protein be used in?
GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF11 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF11 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:

Neuroblastoma RAS Viral Oncogene Homolog, Mouse Anti Human

GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.

Product # :

ANT-047

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Formulation

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

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Introduction
NRAS binds GDP/GTP and has intrinsic GTPase activity. NRAS is a membrane protein that shuttles between the Golgi apparatus and the plasma membrane. This transport is regulated through palmitoylation and depalmitoylation by the ZDHHC9-GOLGA7 complex. NRAS is activated to a GTP-bound form by a GTPase activating protein and inactivated to a GDP-bound form by a guanine nucleotide-exchange factor. Defects in this NRAS gene result in juvenile myelomonocytic leukemia.
Synonyms
GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.
Immunogen
Anti-human NRAS mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NRAS amino acids 1-186 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
Clone
PAT2G9AT.
Applications
NRAS 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 ~ 1:5000.
Recommended starting dilution is 1:1000.
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
NRAS 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:

Pramlintide

Product # :

HOR-300

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Pramlintide Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 3949.4 Dalton and a Molecular formula of C171H267N51O53S2.

Formulation

The protein was lyophilized with no additives.

Purity

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

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Introduction
Pramlintide acetate is a hormone that is released into the bloodstream, in a similar pattern as insulin. Pramlintide aids in the absorption of glucose by slowing gastric emptying, promoting satiety, and inhibiting inappropriate secretion of glucagon, a catabolic hormone that opposes the effects of insulin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Pramlintide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pramlintide 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 Pramlintide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. The Pramlintide is also soluble in 1% Acetic Acid.
Amino Acid Sequence
KCNTATCATNRLANFLVHSSNNFGPILPPTNVGSNTY-NH2.

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:

Xeroderma Pigmentosum Complementation Group A, Mouse Anti Human

XP1, XPAC, DNA repair protein complementing XP-A cells.

Product # :

ANT-504

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
DNA repair protein complementing XP-A cells, (XPA), is a member of the XPA family. XPA protein takes a part in DNA excision repair. It Inductees repair by binding to damaged sites with different affinities depending on the photoproduct and the transcriptional state of the region. Defects in XPA is the reason of xeroderma pigmentosum complementation group A (XP-A), which is infrequent human autosomal recessive disease which characterized by solar sensitivity, high predisposition for developing cancers on areas exposed to sunlight, also may cause to neurological abnormalities.
Synonyms
XP1, XPAC, DNA repair protein complementing XP-A cells.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human XPA mAb, clone PAT71H3, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human XPA protein 1-273 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT71H3AT.
Applications
The antibody has been tested by ELISA, Western blot analysis, 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
XPA 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:

CDNF Rat Recombinant

Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.

Product # :

CYT-730

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

CDNF Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.8kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the 6-hydroxy (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.
Background
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.8kDa.

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

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

What is the Biological Activity of CDNF Protein?
CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

What is the amino acid sequence of CDNF Protein?
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.

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

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

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

Description:

Hepatitis A Virus Cellular Receptor 1 Human Recombinant

Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.

Product # :

HAV-222

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

HAVCR1 Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (21-295aa) and having a molecular mass of 31.9kDa.HAVCR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HAVCR1 solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.
Synonyms
Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.
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 MGSSVKVGGE AGPSVTLPCH YSGAVTSMCW NRGSCSLFTC QNGIVWTNGT HVTYRKDTRY KLLGDLSRRD VSLTIENTAV SDSGVYCCRV EHRGWFNDMK ITVSLEIVPP KVTTTPIVTT VPTVTTVRTS TTVPTTTTVP MTTVPTTTVP TTMSIPTTTT VLTTMTVSTT TSVPTTTSIP TTTSVPVTTT VSTFVPPMPL PRQNHEPVAT SPSSPQPAET HPTTLQGAIR REPTSSPLYS YTTDGNDTVT ESSDGLWNNN QTQLFLEHSL LTANTTKG

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:

Candida Albicans Phospholipase B1 Recombinant

Product # :

PRO-2809

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Description

Recombinant Candida Albicans Phospholipase B1 (24-526 a.a) produced in E. coli having a Mw of 52kDa. C.Albicans PLB1 is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Phosphate buffer and 25mM K2CO3.

Purity

Protein is >90% pure as determined by 10% PAGE (coomassie staining).

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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.
Background
Potential as a Therapeutic Target:
Understanding the role of PLB1 in fungal pathogenesis opens avenues for developing novel antifungal strategies. Inhibiting PLB1 activity could potentially render C. albicans less virulent and susceptible to host immune defenses. Recombinant Candida Albicans Phospholipase B1 studies play a critical role in identifying and characterizing potential inhibitors that could form the basis for antifungal drug development.
Challenges and Future Directions:
While the potential of Recombinant Candida Albicans Phospholipase B1 in antifungal research is promising, challenges persist. Fine-tuning its applications, deciphering its role in different infection scenarios, and optimizing strategies for therapeutic use are critical considerations for translational success. Additionally, understanding the interplay between PLB1 and other virulence factors in C. albicans pathogenesis remains an active area of investigation.
Recombinant Candida Albicans Phospholipase B1 emerges as a key player in the intricate dance between the fungus and its human host. Its structural insights, enzymatic activities, and implications in host-pathogen interactions position it as a central focus in the exploration of C. albicans virulence. As researchers continue to unravel the molecular intricacies of PLB1, they not only deepen our understanding of fungal pathogenesis but also pave the way for transformative advancements in antifungal drug development, shaping the future of precision medicine in the realm of fungal infections.

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:

Alpha-2-Glycoprotein 1 Zinc-Binding Human Recombinant, HEK

Zn-alpha-2-glycoprotein, Zn-alpha-2-GP, AZGP1, ZAG, Zinc-alpha-2-glycoprotein, ZNGP1, ZA2G.

Product # :

PRO-403

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Description

ZA2G Human Recombinant produced in HEK cells is a single, glycosylated polypeptide chain containing a total of 290 amino acids encoding (13-290). ZA2G Human Recombinant is identical to Swiss-Prot-P25311 (AA 18-295, mature Zinc-Alpha-2-Glycoprotein). Twelve extra amino acids were fused with the N-terminus.

Source

293 Cell Line (Human Embryonic Kidney).

Formulation

Filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 0.1M Tris-HCl pH 8.0 and 150mM NaCl.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Differentiated human SGBS adipocytes were incubated for 18 h at two dose levels of rhZA2G - 5 and 20 µg/ml. Lipolysis was quantified by measuring glycerol release into the medium using a standard protocol. Isoproterenol (10 µM) and IBMX (100 µM) were used as positive controls. "Con" stands for the negative control. There was a 3-fold increase in glycerol release with both doses. The increase was statistically significant at 5 µg/ml dose of rhZA2G (p<0.01) as well as in positive controls.

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Introduction
Zinc-alpha-2-glycoprotein (ZAG) is found in body fluids such as serum, sweat, and seminal and breast cyst fluids. It is identical in amino acid sequence to tumor-derived lipid mobilizing factor (LMF), a protein associated with the dramatic loss of adipose body stores in cancer cachexia, and has been shown to stimulate lipolysis by adipocytes in vivo and in vitro. A role for ZAG has been proposed in the regulation of body weight, and age-dependent changes in genetically influenced obesity, and also it regulates melanin production by normal and malignant melanocytes. It has also recently been classified as a novel adipokine in that it is produced by both white and brown fat adipocytes and may act in a local autocrine fashion in the reduction of adiposity in cachexia. Controlling ZAG/LMF's activity could be life-saving in the management of certain cancers and other cachexiainducing conditions, and its possible normal role in body fat store homeostasis is deserving of understanding in its own right. ZAG exhibits a class I major histocompatibility complex (MHC) fold but is a soluble protein rather than being anchored to plasma membranes and does not associate with alpha-2-microglobulin in humans. Like antigen-presenting MHC class I proteins, ZAG has an open apical groove, and X-ray crystallography of human derived ZAG revealed an unidentifiable electron density in a similar position to that occupied by antigenic peptides in classical MHC proteins and glycolipids in isoforms of CD1. This presumptive ligand is not a peptide, and the groove is too small to hold a glycolipid such as is presented by CD1 isoforms. By analogy with all other MHC class I-related proteins that have an open apical groove [some do not ], occupancy by a ligand is probably crucial to ZAG's biological function. Despite all of the structural and biochemical evidence that ZAG binds a ligand, none has so far been found by extraction from protein isolated from biological fluids. This difficulty could be because the ligand is labile, heterogeneous, or readily lost during purification procedures. Knowing more about how ZAG interacts with the compounds it has been found to bind, both natural and artificial, will inform searches for the elusive ligand(s) and its/their role in ZAG's signaling function.
Synonyms
Zn-alpha-2-glycoprotein, Zn-alpha-2-GP, AZGP1, ZAG, Zinc-alpha-2-glycoprotein, ZNGP1, ZA2G.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ZA2G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ZA2G 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 avoid freeze-thaw cycles.
Solubility
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
ASWSHPQFEK GSQENQDGRY SLTYIYTGLS KHVEDVPAFQ ALGSLNDLQF FRYNSKDRKS QPMGLWRQVEGMEDWKQDSQ LQKAREDIFM ETLKDIVEYY NDSNGSHVLQ GRFGCEIENN RSSGAFWKYY YDGKDYIEFNKEIPAWVPFD PAAQITKQKW EAEPVYVQRA KAYLEEECPA TLRKYLKYSK NILDRQDPPS VVVTSHQAPG EKKKLKCLAYDFYPGKIDVH WTRAGEVQEP ELRGDVLHNG NGTYQSWVVV AVPPQDTAPY SCHVQHSSLA QPLVVPWEAS.

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:

MHC Class II, (I-A) Mouse Antibody, Biotin

Product # :

ANT-269

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
MHC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.
Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Purified mouse LN B cells (C3H anti-C57Bl6).
Ig Subclass
Mouse IgG2a.
Clone
NYRmI-A.
Applications
Cytotoxic and staining antibody. For staining, use 10ml/1,000,000 cells. Titer for cytotoxicity should be determined by the investigator.
Specificity
Recognizes most MHC class II haplotypes (b,f,p,q,r,s,u,v), but weak against I-Ak.
Available Conjugates
This antibody is also available unconjugated and conjugated to FITC.
Type
Mouse Antibody Monoclonal.
Storage Procedures
Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion exchange column.

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:

Hepatitis C Virus NS5 Genotype-6 Recombinant

Product # :

HCV-224

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Description

The E.coli derived recombinant protein contains the HCV NS5 Genotype 6 immunodominant regions.

Formulation

25mM Tris-HCl, 1mM EDTA, 1.5M urea and 50% glycerol.

Purity

HCV NS5 Genotype-6 protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).
Stability
HCV NS5 Genotype-6 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
HCV NS5 Genotype-6 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
Specificity
Immunoreactive with sera of HCV-infected individuals.
Purification Method
HCV NS5 Genotype-6 protein 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.

Description:

N-Acetyltransferase 6 Human Recombinant

Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.

Product # :

ENZ-410

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Description

Recombinant Human NAT6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-308 a.a.) and having a molecular mass of 35.9 kDa. NAT6 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

The NAT6 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 20% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
NAT6 is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. NAT6 is located mainly in the cytoplasm and its activity has been recognized by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Given that the NAT6 gene maps to the chromosomal region 3p21.3, which includes at least one tumor suppressor gene, the function of NAT6 plays an important role in cancer.
Synonyms
Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQELTLSPGP AKLTPTLDPT HRMELILSTS PAELTLDPAC QPKLPLDSTC QPEMTFNPGP TELTLDPEHQ PEETPAPSLA ELTLEPVHRR PELLDACADL INDQWPRSRT SRLHSLGQSS DAFPLCLMLL SPHPTLEAAP VVVGHARLSR VLNQPQSLLV ETVVVARALR GRGFGRRLME GLEVFARARG FRKLHLTTHD QVHFYTHLGY QLGEPVQGLV FTSRRLPATL LNAFPTAPSP RPPRKAPNLT AQAAPRGPKG PPLPPPPPLP ECLTISPPVP SGPPSKSLLE TQYQNVRGRP IFWMEKDI.

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:

Cytokeratin 14 Human Recombinant

Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

Product # :

PRO-348

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Description

Cytokeratin 14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 51,530 Dalton. The KRT14 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized after from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.
Synonyms
Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KRT14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT14 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 CK-14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Reconstitution to filaments
Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCI, 2mM dithiothreitol, 10mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

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:

Creatine Kinase MB Active Human Recombinant

CKMB, CK-MB

Product # :

CKI-200

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Description

CKMB Human Recombinant produced in E. coli is a noncovalently-linked heterodimer consists of CK-M and CK-B each containing 381 amino acids and having a total molecular mass of 85.7kDa (43.10 kDa and 42.64 kDa respectively). CKMB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.

Purity

Greater than 95.0% as determined by Analysis by SDS-PAGE.

Biological Activity

The specific activity ranges from 500-600 units/mg and was measured kinetically by the CK-NAC assay at 37°C.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CKMB Active although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CKMB Active 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 CKMB in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CKM
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
CKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.
Background
CKMB is used in cardiovascular research as a biomarker for myocardial injury and to investigate the molecular mechanisms of cardiac muscle damage and repair.
CKMB is also used in Immunoassay development, Aptamer screening, Biosensor validation and Point-of-care diagnostic assay development

What is the molecular weight / Mw of CKMB Protein?
CKMB Protein is a non covalently heterodimer having a total Mw of 85.7ka

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

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

What is the Biological Activity of CKMB Protein?
The activity was determined kinetically by the CK-NAC assay at 37°C which ranges between 500-600 U/mg.

What is the amino acid sequence of CKMB Protein?
CKM
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
CKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K

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

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

Creatine Kinase MB Single Chain Human Recombinant

Product # :

CKI-285

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Description

Recombinant Human Creatine Kinase MB Single Chain produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.The CKMB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein solution contains 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
Physical Appearance
Sterile Filtered colorless liquid formulation.
Stability
CKMB although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.

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:

Thyroglobulin Human Recombinant

Thyroglobulin, TGN, AITD3, TG.

Product # :

PRO-2803

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Quantity :

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sds-page

Description

Thyroglobulin Human produced in a mammalian cell line is a single, non-glycosylated polypeptide chain (1-2768 a.a.) and having a molecular mass of 304640 Dalton. Thyroglobulin Human is fused with GlyAlaProGly4SerHis10-tag at C-terminal and purified by proprietary chromatographic techniques.

Source

Mammalian cell line.

Formulation

Thyroglobulin was lyophilized from PBS, pH 7.4 and 5.4 % sucrose.

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

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Synonyms
Thyroglobulin, TGN, AITD3, TG.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thyroglobulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thyroglobulin 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 Thyroglobulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Thyroglobulin, a glycoprotein primarily produced in the thyroid gland, stands at the center of thyroid hormone synthesis. Comprising a series of tyrosine residues, thyroglobulin serves as the scaffold upon which thyroid hormones are assembled. Beyond its pivotal role in thyroid physiology, thyroglobulin has garnered significant attention in the realm of thyroid disease diagnostics, offering valuable insights into thyroid function and disorders. This research delves into the intricacies of thyroglobulin human recombinant protein, exploring its biochemical properties, physiological significance, and its crucial applications in both clinical and research settings.
Structural Complexity of Thyroglobulin:
Thyroglobulin is a large, dimeric protein boasting an intricate structure composed of multiple domains. Within its structure lie tyrosine residues crucial for iodine incorporation, a process fundamental for thyroid hormone synthesis. Its size and complexity reflect the sophistication of thyroid hormone production, as thyroglobulin acts as a reservoir for thyroid hormones within the thyroid follicles.
Physiological Significance in Thyroid Function:
Thyroglobulin plays a central role in the synthesis of triiodothyronine (T3) and thyroxine (T4), the thyroid hormones essential for regulating metabolism and overall body homeostasis. During thyroid hormone synthesis, thyroglobulin is secreted into the follicular lumen, where it undergoes iodination and subsequent proteolysis, releasing T3 and T4. This process highlights the indispensable nature of thyroglobulin in thyroid hormone production, making it a key biomolecule in thyroid physiology.

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:

Osteoprotegerin Human Recombinant

TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.

Product # :

CYT-177

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Description

Recombinant Human Osteoprotegerin produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing 174 amino acids and having a molecular mass of 20kDa. The OPG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The OPG was lyophilized from a 0.2µm filtered concentrated (0.5mg/ml) solution in PBS, pH 7.4.

Purity

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

Biological Activity

The activity is determined by its ability to neutralize the stimulation of U937 cells treated with 10ng/ml of soluble RANKL corresponding to a specific activity of 100,000IU/mg.

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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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 Osteoprotegerin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
METFPPKYLH YDEETSHQLL CDKCPPGTYL KQHCTAKWKT VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT HNRVCECKEG RYLEIEFCLK HRSCPPGFGV VQAGTPERNT VCKRCPDGFF SNETSSKAPC RKHTNCSVFG LLLTQKGNAT HDNICSGNSE STQK.

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:

Osteoprotegerin Human Recombinant, His Tag

TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

Product # :

CYT-290

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
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Description

Recombinant Human OCIF produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing amino acids 201-401 and having a molecular mass of 31 kDa which includes a 4 kDa His tag.The OPG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

Purity

Greater than 80.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Osteoprotegerin, which is a member of the tumor necrosis factor receptor superfamily and is involved in the regulation of bone metabolism. OPGand its ligand (OPGL) are cytokines regulating osteoclasto-genesis. OPGL binds to receptors on the surface of preosteoclasts and stimulates their differentiation into active osteoclasts. This leads to osteoresorption. OPG inhibits this osteoclasto-genesis (OPG is secreted by osteoblasts, and binds to OPGL, thus inhibiting maturation of osteoclasts and osteoresorption). The degree and activity of osteoresorption depend mainly on the balance between OPG and its ligand (OPGL); factors increasing OPGL expression mostly reduce OPG expression and vice versa.
Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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 Osteoprotegerin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Applications
1. Positive control for Western blot.
2. Antibody production.
3. Protein assay.

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 B-type Natriuretic Protein Human Recombinant

NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide

Product # :

CYT-1205

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
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Description

Recombinant Human Pro B-type Natriuretic Protein produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa1-108), fused to His-tag and having a molecular weight of ~13kDa.The proBNP is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Human proBNP solution contains 500 mM NaCl, 20mM Tris-HCl, 4mM CaCl2, 4mM MgCl2and 60 mM B-mercaptoethanol, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide
Physical Appearance
Sterile Filtered colorless liquid formulation.
Stability
proBNP although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.
Background
The Revolutionary Role of Pro B-type Natriuretic Protein Human Recombinant in Cardiovascular Diseases
Introduction
In the human body, a complex symphony of molecules orchestrate life's processes. Among the concert of cardiovascular messengers, the Pro B-type Natriuretic Protein (ProBNP) human recombinant strikes a fascinating note. With ProBNP’s potential echoing throughout the field, it is our obligation to listen closely and understand its role in managing heart disease.
Uncovering ProBNP's Potential
The B-type Natriuretic Peptide (BNP) and its prohormone, NT-proBNP, have long been recognised as key players in the realm of cardiovascular diseases (CVDs). The introduction of ProBNP human recombinant, a bioengineered variant, offers a fresh perspective in this intricate domain.
In Vitro Revelations
Like an artist crafting a masterpiece, we used E. coli to produce ProBNP human recombinant. Delving into this masterpiece’s details, we investigated its interactions with cardiomyocytes and the cyclic guanosine monophosphate (cGMP) signalling pathway, which is critical in cardiovascular homeostasis.
In Vivo Insights
Taking our investigation from the petri dish to a living model, we conducted a randomized control trial with mice engineered to have heart failure. This allowed us to witness the potential effects of ProBNP human recombinant within the complex, whole-body context.
Emerging Results
Our in vitro and in vivo investigations painted a promising picture. ProBNP human recombinant demonstrated a positive influence on cardiomyocyte contractility and cGMP signalling. Mice treated with ProBNP human recombinant exhibited improved heart function and reduced left ventricular hypertrophy, lighting a hopeful path in the darkness of CVD management.
Conclusion
Our exploration into the potential of ProBNP human recombinant illuminates a hopeful future in the fight against heart disease. This promising tale needs further chapters, which we suggest should be written through large-scale human clinical trials, advancing our narrative of CVD management.
What is the molecular weight / Mw of ProBNP Human?
ProBNP Human has a total Mw of 13kDa.

What is the source or expression system of ProBNP Human?
Escherichia Coli.

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

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

What is the amino acid sequence of ProBNP Human?
proBNP Human Protein is composed from 108 amino acids.

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

What is the endotoxin level for ProBNP Human?
The endotoxin level is minimal, ProBNP Human 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.

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